Quality control product for detecting vaginal secretion and preparation method thereof

Abstract

The invention provides a quality control product for detecting vaginal secretion and a preparation method of the quality control product. The quality control product comprises a negative quality control product and a positive quality control product; the positive quality control product comprises 20-200 mM of a second basic buffer solution, 1-5% of a second enzyme protective agent, 0-0.04% of lactic acid, 0-0.005% of hydrogen peroxide, 0.01-0.1 U / mL of a second leukocyte esterase item, 0.02-0.1 U / mL of sialidase, 0.05-0.5 U / mL of a second N-acetylglucosaminidase item, 50-200 U / mL of a second oxidase item, 2-40 U / mL of a second coagulase item, 50-200 U / mL of beta-glucuronidase, 5-20 U / mL of proline aminopeptidase, 1-5 U / mL of a second alkaline phosphatase item and 0.2-0.2. And 1% of bovine serum albumin.

Description

Technical Field

[0001] This application relates to the field of biopharmaceutical technology, and in particular to a quality control product for detecting vaginal secretions and a method for preparing the same. Background Technology

[0002] Vaginal discharge examination, also known as leukorrhea examination, is a basic procedure in the health examination of the female urinary and reproductive tract. Its main purpose is to detect whether the female urinary and reproductive tract is infected and whether the vaginal environment is normal.

[0003] Currently, the most commonly used method for examining vaginal secretions in clinical practice is the wet slide microscopy. This method has advantages such as ease of operation and rapid detection, and can quickly identify infections caused by fungi, trichomonas, and bacteria, and grade the degree of inflammation to guide clinicians in medication. However, the application of this method also has some limitations, such as: it can only identify the morphology, and the test results are easily affected by external factors such as the uniformity of the smear and the skill level of the examiner.

[0004] To reduce errors caused by the operator's skill level and subjective judgment, and to meet the quality control requirements of laboratory testing, dry chemical multi-sample test strips for vaginitis are gradually being used in clinical practice. Currently, there are many types of dry chemical multi-sample test strips for vaginitis, but the quality control products provided with the test kits are few or unstable, making them unsuitable for widespread adoption.

[0005] Therefore, traditional technologies still need improvement. Summary of the Invention

[0006] Based on this, one or more embodiments of this application provide a quality control product with strong opening stability and capable of quality control of multiple items in vaginal secretion testing, and a method for preparing the same. The technical solution includes:

[0007] According to a first aspect of the embodiments of this application, a quality control product for detecting vaginal secretions is provided, including a negative quality control product and a positive quality control product;

[0008] The negative control, based on its total volume, comprises the following components: 20 mM to 200 mM primary basal buffer, 1% (w / v) to 5% (w / v) primary enzyme protectant, 0.05% (w / v) to 2% (w / v) lactate, 0.01% (w / v) to 5% (w / v) hydrogen peroxide, 0 to 0.005 U / mL primary leukocyte esterase, 0 to 0.01 U / mL sialidase, 0 to 0.04 U / mL primary N-acetylglucosidase, 0 to 45 U / mL primary oxidase, 0 to 1 U / mL primary coagulating enzyme, 0 to 40 U / mL β-glucuronidase, 0 to 4 U / mL primary proline aminopeptidase, and 0 to 0.8 U / mL primary alkaline phosphatase.

[0009] The positive control, based on its total volume, comprises the following components: 20 mM–200 mM second basal buffer, 1% (w / v)–5% (w / v) second enzyme protectant, 0–0.04% (w / v) lactate, 0–0.005% (w / v) hydrogen peroxide, 0.01 U / mL–0.1 U / mL second leukocyte esterase assay, 0.02 U / mL–0.1 U / mL sialidase, and 0.05 U / m The following enzymes were tested: L~0.5U / mL second N-acetylglucosidase, 50U / mL~200U / mL second oxidase, 2U / mL~40U / mL second coagulation enzyme, 50U / mL~200U / mL β-glucuronidase, 5U / mL~20U / mL proline aminopeptidase, 1U / mL~5U / mL second alkaline phosphatase, and 0.2% (w / v)~1% (w / v) bovine serum albumin.

[0010] In one embodiment, at least one of the following conditions (1) to (4) is satisfied:

[0011] (1) The first basic buffer and the second basic buffer are each independently selected from one or more of the following: citrate-sodium citrate buffer solution, acetic acid-sodium acetate buffer solution, disodium hydrogen phosphate-citric acid buffer solution and disodium hydrogen phosphate-sodium dihydrogen phosphate buffer solution;

[0012] (2) The pH of the first basic buffer solution is 3.8 to 4.5;

[0013] (3) The pH of the second basic buffer solution is 5.0–7.0; and

[0014] (4) The first enzyme protectant and the second enzyme protectant are each independently selected from one or more of glycerol, D-sorbitol, mannitol, D-trehalose and sucrose.

[0015] In one embodiment, the first leukocyte esterase and the second leukocyte esterase are each independently selected from one or more of prions, porcine liver esterase, lipase, papain, and acylated amino acid hydrolases.

[0016] In one embodiment, the first N-acetylglucosidase item and the second N-acetylglucosidase item are each independently selected from one or more of N-acetylglucosidase, cellulase, amylase, figase and acylated amino acid hydrolase.

[0017] In one embodiment, the first oxidase and the second oxidase are each independently selected from one or more of ascorbic acid oxidase and L-amino acid oxidase.

[0018] In one embodiment, the first coagulase and the second coagulase are each independently selected from one or more of trypsin, streptoprotein E, pectinase, amylase, and elastase.

[0019] In one embodiment, the first alkaline phosphatase and the second alkaline phosphatase are each independently selected from one or more alkaline phosphatases and acylated amino acid hydrolases.

[0020] In one embodiment, the components of the negative control product, based on the total volume of the negative control product, further include: 0.01% (w / v) to 0.2% (w / v) of a first preservative;

[0021] Optionally, the first preservative includes ProClin300.

[0022] In one embodiment, the positive control sample, based on its total volume, further comprises 0.01% (w / v) to 0.2% (w / v) of a second preservative;

[0023] Optionally, the second preservative includes ProClin300.

[0024] According to a second aspect of the embodiments of this application, a method for preparing a quality control sample for detecting vaginal secretions is provided, comprising the following steps:

[0025] Provide the components of the above-mentioned quality control materials to prepare negative and positive quality control materials respectively;

[0026] The negative control and the positive control were vacuum dried to prepare lyophilized powder of positive control and lyophilized powder of negative control.

[0027] Compared with traditional technologies, this application has the following advantages:

[0028] The quality control products provided in this application can simultaneously control 11 items in vaginal secretion examination (hydrogen peroxide, lactate, leukocyte esterase, sialidase, glucuronidase, proline aminopeptidase, acetylglucosidase, oxidase, coagulation enzyme, alkaline phosphatase, and pH), and have a wide range of applications; at the same time, the positive control products of this application have good opening stability and long-term storage stability. Attached Figure Description

[0029] To more clearly illustrate the technical solutions in the specific embodiments of this application or the prior art, the drawings used in the description of the specific embodiments or the prior art will be briefly introduced below. Obviously, the drawings described below are some embodiments of this application. For those skilled in the art, other drawings can be obtained from these drawings without creative effort.

[0030] Figure 1 A graph showing the positive control results of positive control samples containing different types of leukocyte esterases.

[0031] Figure 2 This is a diagram showing the negative quality control results of an embodiment of this application;

[0032] Figure 3 The graph shows the positive control results of positive control samples containing different concentrations of leukocyte esterase.

[0033] Figure 4 This is a graph showing the positive control results for positive control samples containing different types of oxidases.

[0034] Figure 5 This is a graph showing the positive control results for a project containing different concentrations of oxidase.

[0035] Figure 6 This is a graph showing the positive control results for positive control samples containing different types of coagulating enzymes.

[0036] Figure 7 This is a graph showing the positive control results for a project containing different concentrations of coagulase.

[0037] Figure 8 This is a graph showing the positive control results of positive control samples containing different types of N-acetylglucosidase.

[0038] Figure 9 The graph shows the positive control results of positive control samples containing different concentrations of N-acetylglucosidase.

[0039] Figure 10This is a graph showing the positive control results for positive control samples containing different types of alkaline phosphatase.

[0040] Figure 11 This is a graph showing the positive control results for a test sample containing different concentrations of alkaline phosphatase.

[0041] Figure 12 The graph shows the positive control results for positive control samples containing different concentrations of bovine serum albumin.

[0042] Figure 13 This is a graph showing the positive control results of the positive control sample prepared in Comparative Example 1 of this application;

[0043] Figure 14 This is a graph showing the positive control results of the positive control sample prepared in Comparative Example 2 of this application. Detailed Implementation

[0044] To make the above-mentioned objectives, features, and advantages of this application more apparent and understandable, a detailed description of specific embodiments of this application is provided. Many specific details are set forth in the following description to provide a thorough understanding of this application. However, this application can be implemented in many other ways different from those described herein, and those skilled in the art can make similar modifications without departing from the spirit of this application. Therefore, this application is not limited to the specific embodiments disclosed below.

[0045] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this application belongs. The terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting of the application. Unless otherwise specifically stated, all raw materials, reagents, instruments, and equipment used in this application are commercially available or can be prepared by existing methods.

[0046] A first aspect of this application provides a quality control product for detecting vaginal secretions, including a negative quality control product and a positive quality control product;

[0047] Based on the total volume of the negative control, the negative control comprises the following components: 20mM–200mM primary basal buffer, 1% (w / v)–5% (w / v) primary enzyme protectant, 0.05% (w / v)–2% (w / v) lactate, 0.01% (w / v)–5% (w / v) hydrogen peroxide, 0–0.005 U / mL primary leukocyte esterase, 0–0.01 U / mL sialidase, 0–0.04 U / mL primary N-acetylglucosidase, 0–45 U / mL primary oxidase, 0–1 U / mL primary coagulation enzyme, 0–40 U / mL β-glucuronidase, 0–4 U / mL primary proline aminopeptidase, and 0–0.8 U / mL primary alkaline phosphatase.

[0048] Based on the total volume of the positive control, the positive control comprises the following components: 20mM–200mM second basal buffer, 1% (w / v)–5% (w / v) second enzyme protectant, 0–0.04% (w / v) lactate, 0–0.005% (w / v) hydrogen peroxide, 0.01U / mL–0.1U / mL second leukocyte esterase assay, 0.02U / mL–0.1U / mL sialidase, and 0.05U / mL–0. 0.5 U / mL second N-acetylglucosidase, 50 U / mL to 200 U / mL second oxidase, 2 U / mL to 40 U / mL second coagulase, 50 U / mL to 200 U / mL β-glucuronidase, 5 U / mL to 20 U / mL second proline aminopeptidase, 1 U / mL to 5 U / mL second alkaline phosphatase, and 0.2% (w / v) to 1% (w / v) bovine serum albumin.

[0049] Understandably, the content of each component in the above-mentioned negative and positive quality control products is based on the equivalent content when each component is mixed together. However, the form in which the negative and positive quality control products provided in this application exist is not limited to this. Each component is allowed to be placed separately, as long as they are mixed in the same system when they are to be used.

[0050] Taking lactic acid in the sample to be tested as an example, when its content is high, it can cause the corresponding item in the negative control to develop color but not the corresponding item in the positive control; when its content is low, the corresponding item in the negative control will not develop color.

[0051] Taking sialic anhydrase in the sample to be tested as an example, when its content is high, it can cause the corresponding item in the positive control to develop color but not the corresponding item in the negative control; when its content is low, the corresponding item in the positive control will not develop color.

[0052] In some embodiments, the first basal buffer and the second basal buffer are each independently selected from one or more of the following: citrate-sodium citrate buffer, acetate-sodium acetate buffer, disodium hydrogen phosphate-citrate buffer, and disodium hydrogen phosphate-sodium dihydrogen phosphate buffer.

[0053] In some embodiments, the pH of the first basal buffer is 3.8 to 4.5.

[0054] In some embodiments, the pH of the second basal buffer is 5.0 to 7.0.

[0055] Understandably, the concentrations of the first and second basal buffers in this application are both "20mM to 200mM", meaning they can each independently take the minimum and maximum values ​​within the range of 20mM to 200mM, as well as every value between these minimum and maximum values. Specifically, this includes, but is not limited to, the point values ​​in the embodiments and the following point values: 20mM, 21mM, 22mM, 23mM, 24mM, 25mM, 26mM, 27mM, 28mM, 29mM, 30mM, 40mM, 50mM, 60mM, 70mM, 80mM, 90mM, 100mM, 110mM, 120mM, 130mM, 140mM, 150mM, 160mM, 170mM, 180mM, 190mM, or 200mM; or any range consisting of any two of these values, such as 60mM to 185mM.

[0056] In some optional examples, the concentration of the first basal buffer is 80 mM to 120 mM; more preferably, the concentration of the first basal buffer is 100 mM.

[0057] In some optional examples, the concentration of the second basal buffer is 80 mM to 120 mM; more preferably, the concentration of the second basal buffer is 100 mM.

[0058] In some embodiments, the first enzyme protectant and the second enzyme protectant are each independently selected from one or more of glycerol, D-sorbitol, mannitol, D-trehalose, and sucrose.

[0059] Understandably, the concentrations of the first and second enzyme protectants in this application are both "1% (w / v) to 5% (w / v)," meaning that each can independently take the minimum and maximum values ​​within the range of 1% (w / v) to 5% (w / v), as well as every value between such minimum and maximum values. Specifically, including but not limited to the point values ​​in the embodiments and the following point values: 1% (w / v), 1.1% (w / v), 1.2% (w / v), 1.3% (w / v), 1.4% (w / v), 1.5% (w / v), 1.6% (w / v), 1.7% (w / v), 1.8% (w / v), 1.9% (w / v), 2% (w / v), 2.5% (w / v), 3% (w / v), 3.5% (w / v), 4% (w / v), 4.5% (w / v), or 5% (w / v); or a range consisting of any two of these values, such as 2.2% (w / v) to 4.8% (w / v).

[0060] In some optional examples, the concentration of the first enzyme protectant is 2% (w / v) to 4% (w / v); more optionally, the concentration of the first enzyme protectant is 3% (w / v).

[0061] In some optional examples, the concentration of the second enzyme protectant is 2% (w / v) to 4% (w / v); more optionally, the concentration of the second enzyme protectant is 3% (w / v).

[0062] In some embodiments, the first leukocyte esterase and the second leukocyte esterase are each independently selected from one or more of prions, porcine liver esterase, lipase, papain, and protease.

[0063] Optionally, the first leukocyte esterase item and the second leukocyte esterase item can each be independently selected from one or more of prions and porcine liver esterase; further optionally, the first leukocyte esterase item and the second leukocyte esterase item can each be independently selected from prions or porcine liver esterase.

[0064] Understandably, the concentration of the second leukocyte esterase in the positive control sample of this application is "0.01 U / mL to 0.1 U / mL", which can be the minimum and maximum value of the range of 0.01 U / mL to 0.1 U / mL, as well as every value between the minimum and maximum value. Specifically, this includes, but is not limited to, the point values ​​in the examples and the following point values: 0.01 U / mL, 0.02 U / mL, 0.03 U / mL, 0.04 U / mL, 0.05 U / mL, 0.06 U / mL, 0.07 U / mL, 0.08 U / mL, 0.09 U / mL, or 0.1 U / mL; or any range of any two of these values, such as: 0.015 U / mL to 0.085 U / mL.

[0065] In some optional examples, the concentration of the second leukocyte esterase in the positive control is 0.04 U / mL to 0.06 U / mL; more optionally, the concentration of the second leukocyte esterase in the positive control is 0.05 U / mL.

[0066] Understandably, the concentration of sialidase in the positive control sample of this application is "0.02 U / mL to 0.1 U / mL", which can be the minimum and maximum value of the range of 0.02 U / mL to 0.1 U / mL, as well as every value between the minimum and maximum value. Specifically, this includes, but is not limited to, the point values ​​in the examples and the following point values: 0.02 U / mL, 0.03 U / mL, 0.04 U / mL, 0.05 U / mL, 0.06 U / mL, 0.07 U / mL, 0.08 U / mL, 0.09 U / mL, or 0.1 U / mL; or any range of any two of these values, such as 0.25 U / mL to 0.085 U / mL.

[0067] In some optional examples, the concentration of sialidase in the positive control is 0.04 U / mL to 0.08 U / mL; more optionally, the concentration of sialidase in the positive control is 0.06 U / mL.

[0068] In some embodiments, the first N-acetylglucosidase item and the second N-acetylglucosidase item are each independently selected from one or more of N-acetylglucosidase, cellulase, amylase, figase and acylated amino acid hydrolase.

[0069] Understandably, the concentration of the second N-acetylglucosidase in the positive control sample of this application is "0.05 U / mL to 0.5 U / mL", which can be the minimum and maximum value of the range of 0.05 U / mL to 0.5 U / mL, as well as every value between such minimum and maximum value. Specifically, it includes, but is not limited to, the point values ​​in the examples and the following point values: 0.05 U / mL, 0.06 U / mL, 0.07 U / mL, 0.08 U / mL, 0.09 U / mL, 0.1 U / mL, 0.12 U / mL, 0.14 U / mL, 0.16 U / mL, 0.18 U / mL, 0.2 U / mL, 0.3 U / mL, 0.4 U / mL, or 0.5 U / mL; or any range of any two of these values, such as 0.15 U / mL to 0.35 U / mL.

[0070] In some optional examples, the concentration of the second N-acetylglucosidase in the positive control is 0.1 U / mL to 0.4 U / mL; more optionally, the concentration of the second N-acetylglucosidase in the positive control is 0.25 U / mL.

[0071] In some embodiments, the first oxidase and the second oxidase are each independently selected from one or more of ascorbic acid oxidase and L-amino acid oxidase. Optionally, the second oxidase is selected from ascorbic acid oxidase.

[0072] Understandably, the concentration of the second oxidase in the positive control sample of this application is "50 U / mL to 200 U / mL", which means the minimum and maximum values ​​of the range of 50 U / mL to 200 U / mL, as well as every value between the minimum and maximum values. Specifically, this includes, but is not limited to, the point values ​​in the examples and the following point values: 50 U / mL, 51 U / mL, 52 U / mL, 53 U / mL, 54 U / mL, 55 U / mL, 56 U / mL, 57 U / mL, 58 U / mL, 59 U / mL, 60 U / mL, 70 U / mL, 80 U / mL, 90 U / mL, 100 U / mL, 110 U / mL, 120 U / mL, 130 U / mL, 140 U / mL, 150 U / mL, 160 U / mL, 170 U / mL, 180 U / mL, 190 U / mL, or 200 U / mL; or any range of any two of these values, such as 65 U / mL to 185 U / mL.

[0073] In some optional examples, the concentration of the second oxidase in the positive control is 80 U / mL to 150 U / mL; more optionally, the concentration of the second oxidase in the positive control is 100 U / mL.

[0074] In some embodiments, the first coagulase and the second coagulase are each independently selected from one or more of trypsin, streptoprotein E, pectinase, amylase, and elastase.

[0075] Optionally, the first coagulase and the second coagulase are each independently selected from one or more of trypsin and streptoprotein E; more preferably, the first coagulase and the second coagulase are each independently selected from trypsin or streptoprotein E.

[0076] Understandably, the concentration of the second coagulase in the positive control sample of this application is "2 U / mL to 40 U / mL", which means the minimum and maximum values ​​within the range of 2 U / mL to 40 U / mL, as well as every value between these minimum and maximum values. Specifically, this includes, but is not limited to, the point values ​​in the examples and the following point values: 2 U / mL, 3 U / mL, 4 U / mL, 5 U / mL, 6 U / mL, 7 U / mL, 8 U / mL, 9 U / mL, 10 U / mL, 11 U / mL, 12 U / mL, 13 U / mL, 14 U / mL, 15 U / mL, 16 U / mL, 17 U / mL, 18 U / mL, 19 U / mL, 20 U / mL, 25 U / mL, 30 U / mL, 35 U / mL, or 40 U / mL; or any range consisting of any two of these values, such as 5.5 U / mL to 32.5 U / mL.

[0077] In some optional examples, the concentration of the second coagulase in the positive control is 10 U / mL to 30 U / mL; more optionally, the concentration of the second coagulase in the positive control is 20 U / mL.

[0078] Understandably, the concentration of β-glucuronidase in the positive control sample of this application is "50 U / mL to 200 U / mL", which means taking the minimum and maximum values ​​of the range of 50 U / mL to 200 U / mL, as well as every value between such minimum and maximum values. Specifically, this includes, but is not limited to, the point values ​​in the examples and the following point values: 50 U / mL, 51 U / mL, 52 U / mL, 53 U / mL, 54 U / mL, 55 U / mL, 56 U / mL, 57 U / mL, 58 U / mL, 59 U / mL, 60 U / mL, 70 U / mL, 80 U / mL, 90 U / mL, 100 U / mL, 110 U / mL, 120 U / mL, 130 U / mL, 140 U / mL, 150 U / mL, 160 U / mL, 170 U / mL, 180 U / mL, 190 U / mL, or 200 U / mL; or any range of any two of these values, such as 55 U / mL to 188 U / mL.

[0079] In some optional examples, the concentration of β-glucuronidase in the positive control is 100 U / mL to 150 U / mL; more optionally, the concentration of β-glucuronidase in the positive control is 125 U / mL.

[0080] Understandably, the concentration of proline aminopeptidase in the positive control sample of this application is "5 U / mL to 20 U / mL", which means the minimum and maximum value of the range of 5 U / mL to 20 U / mL, as well as every value between the minimum and maximum value. Specifically, this includes, but is not limited to, the point values ​​in the examples and the following point values: 5 U / mL, 6 U / mL, 7 U / mL, 8 U / mL, 9 U / mL, 10 U / mL, 11 U / mL, 12 U / mL, 13 U / mL, 14 U / mL, 15 U / mL, 16 U / mL, 17 U / mL, 18 U / mL, 19 U / mL, or 20 U / mL; or any range of any two of these values, such as 5.25 U / mL to 18.5 U / mL.

[0081] In some optional examples, the concentration of proline aminopeptidase in the positive control is 10 U / mL to 15 U / mL; more optionally, the concentration of proline aminopeptidase in the positive control is 12.5 U / mL.

[0082] In some embodiments, the first alkaline phosphatase and the second alkaline phosphatase are each independently selected from one or more alkaline phosphatases and acylated amino acid hydrolases.

[0083] Understandably, the concentration of the second alkaline phosphatase in the positive control sample of this application is "1 U / mL to 5 U / mL", which means taking the minimum and maximum value of the range of 1 U / mL to 5 U / mL, as well as every value between the minimum and maximum value. Specifically, it includes, but is not limited to, the point values ​​in the examples and the following point values: 1 U / mL, 1.1 U / mL, 1.2 U / mL, 1.3 U / mL, 1.4 U / mL, 1.5 U / mL, 1.6 U / mL, 1.7 U / mL, 1.8 U / mL, 1.9 U / mL, 2 U / mL, 3 U / mL, 4 U / mL, or 5 U / mL; or any range of any two of these values, such as 1.5 U / mL to 4.5 U / mL.

[0084] In some optional examples, the concentration of the second alkaline phosphatase in the positive control is 2 U / mL to 4 U / mL; more optionally, the concentration of the second alkaline phosphatase in the positive control is 3 U / mL.

[0085] In this application, the concentration of bovine serum albumin is "0.2% (w / v) to 1% (w / v)," which can be the minimum and maximum value within the range of 0.2% (w / v) to 1% (w / v), as well as every value between the minimum and maximum value. Specifically, it includes, but is not limited to, the point values ​​in the examples and the following point values: 0.2% (w / v), 0.3% (w / v), 0.4% (w / v), 0.5% (w / v), 0.6% (w / v), 0.7% (w / v), 0.8% (w / v), 0.9% (w / v), or 1% (w / v); or any range consisting of any two of these values, such as 0.25% (w / v) to 0.85% (w / v).

[0086] In some optional examples, the concentration of bovine serum albumin is 0.4% (w / v) to 0.8% (w / v); more optionally, the concentration of bovine serum albumin is 0.6% (w / v).

[0087] In some embodiments, the components of the negative control product, based on the total volume of the negative control product, further include: 0.01% to 0.2% (w / v) of a first preservative.

[0088] Optionally, the concentration of the first preservative is 0.1% (w / v).

[0089] In some embodiments, the positive control product, based on its total volume, further comprises 0.01% to 0.2% (w / v) of a second preservative.

[0090] Optionally, the concentration of the second preservative is 0.1% (w / v).

[0091] In some optional examples, both the first and second preservatives are selected from ProClin300.

[0092] The quality control products described in this application can simultaneously control 11 items (hydrogen peroxide, lactate, leukocyte esterase, sialidase, glucuronidase, proline aminopeptidase, acetylglucosidase, oxidase, coagulation enzyme, alkaline phosphatase, and pH) when testing vaginal secretions, and the test results of each item do not interfere with each other. In particular, the opening stability of the β-glucuronidase item has been improved. In addition, by adjusting and improving the components and concentrations of the negative and positive quality control products, this application enables the quality control products to have good opening stability and long-term stability.

[0093] A second aspect of this application provides a method for preparing a quality control sample for detecting vaginal secretions, comprising steps S10 to S20.

[0094] Step S10: Provide the components of the above-mentioned quality control materials to prepare negative and positive quality control materials respectively.

[0095] In some embodiments, the components of the positive control and the negative control are as described in the first aspect above, and will not be repeated here.

[0096] Step S20: Vacuum dry the negative control sample and the positive control sample respectively to prepare lyophilized powder of positive control sample and lyophilized powder of negative control sample.

[0097] In some embodiments, the vacuum drying temperature is 24°C to 26°C; alternatively, the vacuum drying temperature is 25°C.

[0098] In some embodiments, the vacuum drying time is 1 to 2 hours; alternatively, the vacuum drying time is 1.5 hours.

[0099] In this application, negative and positive quality control samples are prepared into lyophilized powders, which are then reconstituted before use, thereby effectively improving the long-term stability of the positive quality control samples.

[0100] The present application will be further described below with reference to specific embodiments and comparative examples, but these should not be construed as limiting the scope of protection of the present application. Unless otherwise specified, the raw materials involved in the following specific embodiments are all commercially available, the instruments used are all commercially available, and the processes involved are conventionally selected by those skilled in the art unless otherwise specified.

[0101] Example 1: The impact of different leukocyte esterase assays on quality control results

[0102] (1) The impact of different types of leukocyte esterase tests on positive quality control results

[0103] a) Preparation of positive control samples: 100 mM citrate-sodium citrate buffer solution, 3% (w / v) D-sorbitol, 0.1% (w / v) ProClin 300, 0.02% (w / v) lactic acid, 0.003% (w / v) hydrogen peroxide, 0.05 U / mL leukocyte esterase (selecting prions, porcine liver esterase, porcine pancreatic lipase, papain, and subtilisin as leukocyte esterase, respectively, to prepare positive control samples 1-5), 0.05 U / mL sialidase, and 0.25 U / mL... N-acetylglucosidase, 100 U / mL ascorbic acid oxidase, 20 U / mL trypsin, 100 U / mL β-glucuronidase, 10 U / mL proline aminopeptidase, 3 U / mL alkaline phosphatase, and 0.6% bovine serum albumin were mixed thoroughly to obtain a positive control solution. The positive control solution was then vacuum-dried at 25°C for 1.5 h to obtain positive control samples 1–5.

[0104] b) Preparation of negative control: Mix 100mM citrate-sodium citrate buffer solution, 3% (w / v) D-sorbitol, 0.1% (w / v) ProClin300, 1% (w / v) lactic acid, 0.1% (w / v) hydrogen peroxide, 0.003U / mL prionase, 0.005U / mL sialidase, 0.002U / mL N-acetylglucosidase, 20U / mL ascorbic acid oxidase, 0.2U / mL trypsin, 10U / mL β-glucuronidase, 2U / mL proline aminopeptidase, and 0.3U / mL alkaline phosphatase to obtain the negative control solution.

[0105] c) The positive control samples 1-5 prepared above were used in the combined vaginitis detection kit (dry chemical enzymatic method) (manufacturer: AVE-11A, AV Technology Co., Ltd.); the testing instrument was the reproductive tract secretion analyzer (AVE-320, AV Technology Co., Ltd.); the quality control test results of positive control samples 1-5 are shown in Table 1 and Figure 1 As shown in Figure a.

[0106] The negative control sample prepared above was used to test the combined detection kit for vaginitis, and the results are as follows: Figure 2 As shown.

[0107] The positive control samples 1-5 obtained above were placed at 4℃ for 7 days and then tested again on the vaginitis combined detection kit to test its open-open stability; the open-open stability results are as follows. Figure 1 As shown in b.

[0108] In Table 1, "+" indicates that the test result is positive; "-" indicates that the test result is negative.

[0109] Table 1

[0110]

[0111] As shown in Table 1, lipase, papain, and subtilisin, while meeting the requirement for positive color development of the leukocyte esterase test, can affect the color development of the β-glucuronidase test, resulting in no color development of the β-glucuronidase test. In contrast, prions and porcine liver esterase, while meeting the requirement for positive color development of the leukocyte esterase test, do not affect the color development results of other tests, and their stability after opening reaches 7 days, meeting the requirements.

[0112] (2) The effect of leukocyte esterase concentration on positive quality control results

[0113] The process is basically the same as step (1), except that the positive control solution is prepared differently: prions with concentrations of 0.005 U / mL, 0.01 U / mL, 0.05 U / mL, 0.1 U / mL and 0.2 U / mL are selected as leukocyte esterases to prepare positive control solutions.

[0114] The positive control solution was vacuum dried at 25°C for 1.5 hours. The quality control test results of the final positive control samples 6-10 are shown in Table 2 and... Figure 3 As shown in Table 2. In Table 2, "-" indicates negative, "±" indicates weak positive, "+" indicates positive, "++" indicates strong positive, and "+++" indicates extremely strong positive.

[0115] Table 2

[0116]

[0117]

[0118] As shown in Table 2, when the concentration of the leukocyte esterase test is 0.005 U / mL, the leukocyte esterase test does not show color development; when the concentration of the leukocyte esterase test is 0.2 U / mL, it affects the color development of the β-glucuronidase test.

[0119] Porcine liver esterase was selected as the leukocyte esterase test and the same concentration gradient was used for detection. The results were the same as those for prions. Therefore, the concentration of the leukocyte esterase test is controlled at 0.01 U / mL to 0.1 U / mL in this application.

[0120] Example 2: The impact of different oxidases on quality control results

[0121] (1) The impact of the type of oxidase on positive quality control results

[0122] The process is basically the same as step (1) in Example 1, except that the preparation of the positive control solution is different: 0.05 U / mL prionase is selected as the leukocyte esterase, and 100 U / mL ascorbic acid oxidase, 0.1 mM copper ions, 0.1 mM iron ions, 0.1 mM TEMPO, 0.1 mM potassium iodate, 0.1 mM potassium periodate and 100 U / mL L-amino acid oxidase are selected as the oxidases to prepare the positive control solution.

[0123] Ascorbic acid oxidase, copper ions, iron ions, TEMPO and its derivatives, potassium iodate, potassium periodate, and L-amino acid oxidase can be used as quality control materials to detect oxidase items individually; therefore, this embodiment selects the above substances in combination with other quality control items.

[0124] The positive control solution was vacuum dried at 25°C for 1.5 hours. The quality control test results of the finally prepared positive control samples 11-17 are shown in Table 3 and... Figure 4 As shown in Figure a; the results of the opening stability after being placed at 4℃ for 7 days are as follows. Figure 4 As shown in b.

[0125] Table 3

[0126]

[0127] Table 3 shows that copper ions, iron ions, TEMPO and its derivatives, potassium iodate, potassium periodate, and L-amino acid oxidase all affect β-glucuronidase activity, resulting in no color development of the β-glucuronidase test, even under the condition of positive color development for the oxidase test. Only ascorbic acid oxidase can simultaneously meet the color development requirements for both the oxidase and β-glucuronidase tests, and also meets the requirement of 7 days of stability after opening.

[0128] (2) The effect of oxidase concentration on positive quality control results

[0129] The process is basically the same as step (1), except that the preparation of the positive control solution is different: ascorbic acid oxidase with concentrations of 20 U / mL, 50 U / mL, 100 U / mL, 200 U / mL and 300 U / mL is selected as the oxidase item, and the positive control solution is prepared.

[0130] The positive control solution was vacuum dried at 25°C for 1.5 hours. The quality control test results of the finally prepared positive control samples 18-22 are shown in Table 4. Figure 5 As shown.

[0131] Table 4

[0132]

[0133] As shown in Table 4, when the concentration of the oxidase is only 20 U / mL, the oxidase does not develop color; when the concentration of the oxidase reaches 300 U / mL, it affects the color development of the β-glucuronidase. Therefore, in this application, the concentration of the oxidase is controlled to be between 50 U / mL and 200 U / mL.

[0134] Example 3: The impact of different coagulating enzymes on quality control results

[0135] (1) The impact of the type of coagulase on positive quality control results

[0136] The process is basically the same as step (1) in Example 1, except that the preparation of the positive control solution is different: 0.05 U / mL prionase is selected as the leukocyte esterase project, and 20 U / mL trypsin, streptoprotein E, pectinase, amylase and elastase are selected as coagulating enzyme projects to prepare the positive control solution.

[0137] The positive control solution was vacuum dried at 25°C for 1.5 h. The quality control test results of the finally prepared positive control samples 23-27 are shown in Table 5. Figure 6 As shown in Figure a; the results of the opening stability after being placed at 4℃ for 7 days are as follows. Figure 6 As shown in b.

[0138] Table 5

[0139]

[0140] Table 5 shows that pectinase, amylase, and elastase, at concentrations sufficient for coagulation enzyme color development, all affect β-glucuronidase activity, resulting in no color development for the β-glucuronidase test. Trypsin and streptoprotein E can simultaneously satisfy both coagulation enzyme and β-glucuronidase color development requirements, while also meeting the requirement of 7 days of stability after opening.

[0141] (2) The effect of coagulation enzyme concentration on positive quality control results

[0142] The process is basically the same as step (1), except that the preparation of the positive control solution is different: trypsin with concentrations of 1 U / mL, 2 U / mL, 20 U / mL, 40 U / mL and 60 U / mL are selected as coagulating enzymes to prepare positive control solutions.

[0143] The positive control solution was vacuum dried at 25°C for 1.5 hours. The quality control test results of the final positive control samples 28–32 are shown in Table 6. Figure 7 As shown.

[0144] Table 6

[0145]

[0146] As shown in Table 6, when the concentration of the coagulase test is 1 U / mL, the coagulase test does not develop color; when the concentration of the coagulase test reaches 60 U / mL, it affects the color development of the β-glucuronidase test.

[0147] Streptomycin E was selected as the coagulant and the same concentration gradient was used for testing, with results identical to those of trypsin. Therefore, the concentration of the coagulant in this application is controlled to be between 2 U / mL and 40 U / mL.

[0148] Example 4: The impact of different N-acetylglucosidase items on quality control results

[0149] (1) The impact of N-acetylglucosidase type on positive quality control results

[0150] The process is basically the same as step (1) in Example 1, except that the preparation of the positive control solution is different: 0.05 U / mL prionase is selected as the leukocyte esterase project, and N-acetylglucosidase, cellulase, amylase, fig protease and acylated amino acid hydrolase with a concentration of 0.25 U / mL are selected as N-acetylglucosidase projects respectively, and the positive control solution is prepared.

[0151] The positive control solution was vacuum dried at 25°C for 1.5 hours. The quality control test results of the final positive control samples 33–38 are shown in Table 7. Figure 8 As shown in Figure a; the results of the opening stability after being placed at 4℃ for 7 days are as follows. Figure 8 As shown in b.

[0152] Table 7

[0153]

[0154] Table 7 shows that amylase, figase, and acylated amino acid hydrolase, under the concentration conditions required for color development in the coagulation enzyme test, all affect β-glucuronidase activity, resulting in no color development for the β-glucuronidase test. N-acetylglucosidase and cellulase can simultaneously meet the color development requirements for both the acetylglucosidase and β-glucuronidase tests, while also satisfying the requirement of 7 days of stability after opening.

[0155] (2) The effect of N-acetylglucosidase concentration on positive control results

[0156] The process is basically the same as step (1), except that the preparation of the positive control solution is different: N-acetylglucosidase with concentrations of 0.04 U / mL, 0.05 U / mL, 0.25 U / mL, 0.4 U / mL and 0.5 U / mL are selected as N-acetylglucosidase items, and positive control solutions are prepared.

[0157] The positive control solution was vacuum dried at 25°C for 1.5 h. The quality control test results of the final positive control samples 39–43 are shown in Table 8. Figure 9 As shown.

[0158] Table 8

[0159]

[0160] As shown in Table 8, when the concentration of N-acetylglucosidase is 0.04 U / mL, the NAG test does not show color development; when the concentration of N-acetylglucosidase reaches 0.5 U / mL, it affects the color development of the β-glucuronidase test. Therefore, in this application, the concentration of N-acetylglucosidase is controlled at 0.05 U / mL to 0.4 U / mL.

[0161] Example 5: The impact of different alkaline phosphatase parameters on quality control results

[0162] (1) The impact of alkaline phosphatase test types on positive quality control results

[0163] The process is basically the same as step (1) in Example 1, except that the positive control solution and the positive control lyophilized powder are prepared differently: 0.05 U / mL prionase is selected as the leukocyte esterase project, and alkaline phosphatase and acylated amino acid hydrolase with a concentration of 3 U / mL are selected respectively to prepare the positive control solution.

[0164] The positive control solution was vacuum dried at 25°C for 1.5 hours. The quality control test results of the final positive control samples 44-45 are shown in Table 9. Figure 10 As shown in Figure a; the results of the opening stability after being placed at 4℃ for 7 days are as follows. Figure 10 As shown in b.

[0165] Table 9

[0166]

[0167]

[0168] As shown in Table 9, acylated amino acid hydrolases, under the concentration conditions required for color development in the coagulation enzyme test, affect β-glucuronidase activity, resulting in no color development in the β-glucuronidase test. Alkaline phosphatase can simultaneously meet the color development requirements for both the alkaline phosphatase and β-glucuronidase tests, while also satisfying the requirement of 7 days of stability after opening.

[0169] (2) The effect of alkaline phosphatase concentration on positive control results

[0170] The process is basically the same as step (1), except that the preparation of the positive control lyophilized powder is different: alkaline phosphatase with concentrations of 0.5 U / mL, 1 U / mL, 3 U / mL, 5 U / mL and 6 U / mL is selected respectively to prepare the positive control solution.

[0171] The positive control solution was vacuum dried at 25°C for 1.5 hours. The quality control test results of the final positive control samples (46-50) are shown in Table 10. Figure 11 As shown.

[0172] Table 10

[0173]

[0174] As shown in Table 10, when the concentration of alkaline phosphatase is 0.5 U / mL, the coagulation enzyme test does not show color; when the concentration of alkaline phosphatase reaches 6 U / mL, it affects the color development of β-glucuronidase. Therefore, in this application, the concentration of alkaline phosphatase is controlled to be between 1 U / mL and 5 U / mL.

[0175] Example 6: The effect of bovine serum albumin on quality control results

[0176] (1) The effect of bovine serum albumin concentration on positive control results

[0177] The procedure is basically the same as step (1) in Example 1, except that the positive control solution and the positive control lyophilized powder are prepared differently: 0.05 U / mL prions are selected as the leukocyte esterase project; bovine serum albumin at concentrations of 0%, 0.2%, 0.6%, 1%, and 2% (w / v) are selected to prepare the positive control solution.

[0178] The positive control solution was vacuum dried at 25°C for 1.5 h. The quality control test results of the finally prepared positive control samples 51-55 are shown in Table 11 and... Figure 12 As shown in Table 11. In Table 11, "-" indicates negative, "±" indicates weak positive, "+" indicates positive, and "++" indicates strong positive.

[0179] Table 11

[0180]

[0181] From Table 11 and Figure 11 It is known that when the concentration of bovine serum albumin is 0.2% (w / v) to 1% (w / v), it enhances the color development of the β-glucuronidase test without affecting the color development of other tests; however, a concentration exceeding 1% (w / v) will affect the color development of both the β-glucuronidase and coagulase tests.

[0182] Example 7: Stability test of positive control sample after opening

[0183] a) Preparation of positive control: 100 mM citrate-sodium citrate buffer solution, 3% (w / v) D-sorbitol, 0.1% (w / v) ProClin300, 0.02% (w / v) lactic acid, 0.003% (w / v) hydrogen peroxide, 0.05 U / mL prions, 0.05 U / mL sialidase, 0.25 U / mL N-acetylglucosidase, 100 U / mL ascorbic acid oxidase, 20 U / mL trypsin, 100 U / mL β-glucuronidase, 10 U / mL proline aminopeptidase, 3 U / mL alkaline phosphatase, and 0.6% (w / v) bovine serum albumin were mixed thoroughly to obtain a positive control solution; the positive control solution was then vacuum-dried at 25 °C for 1.5 h to obtain positive control 56. The positive control sample was reconstituted with pure water and placed at 4°C for 7 days. The quality control results were tested once a day, and the results are shown in Table 12.

[0184] Table 12

[0185]

[0186]

[0187] As shown in the table above, the positive control sample of this application, after being opened and reconstituted, maintains its stability for at least 7 days at 4°C, demonstrating good stability after opening.

[0188] The positive control was stored at 4°C and its quality control results were tested monthly. The results are shown in Table 13.

[0189] Table 13

[0190]

[0191] As shown in the table above, the positive control sample of this application can be stored at 4°C for a long period of time without any change in stability for at least 12 months, indicating good stability.

[0192] Example 8: Opening stability test of negative control samples

[0193] a) Preparation of negative control: 100 mM citrate-sodium citrate buffer solution, 3% (w / v) D-sorbitol, 0.1% (w / v) ProClin 300, 1% (w / v) lactic acid, 0.1% (w / v) hydrogen peroxide, 0.003 U / mL prionase, 0.005 U / mL sialidase, 0.002 U / mL N-acetylglucosidase, 20 U / mL ascorbic acid oxidase, 0.2 U / mL trypsin, 10 U / mL β-glucuronidase, 2 U / mL proline aminopeptidase, and 0.3 U / mL alkaline phosphatase were mixed thoroughly to obtain the negative control solution. The negative control solution was then vacuum-dried at 25 °C for 1.5 h to obtain the negative control. This negative control was reconstituted with pure water and stored at 4 °C for 7 days. The quality control results were tested daily, and the results are shown in Table 14.

[0194] Table 14

[0195]

[0196]

[0197] As shown in the table above, the negative control sample of this application, after being opened and reconstituted, maintains its stability for at least 7 days at 4°C, demonstrating good stability after opening.

[0198] The negative control samples were stored at 4°C, and their quality control results were tested monthly. The results are shown in Table 15.

[0199] Table 15

[0200]

[0201] As shown in the table above, the negative control sample of this application can maintain its stability for at least 12 months without change when stored at 4°C, indicating good stability.

[0202] Comparative Example 1:

[0203] Positive control sample 56 was prepared by mixing the following components: pH 5.0, 200 mmol / L citrate buffer, 0.05 g / L sodium nitrite, 0.01 g / L sodium mercaptopyridine-1-oxide, 50 mmol / L trehalose, 80 mmol / L mannitol, 60 mmol / L 5-hydroxylysine, 200 mmol / L bovine serum albumin, 0.05 g / L gelatin, 2.0 U / mL lactate dehydrogenase, 3.0 U / mL L-amino acid oxidase, 8.0 U / mL galacturonase, 50.0 U / L α-mannosidase, 6.0 U / L chymotrypsin, 125.0 U / mL leukocyte esterase, 18.0 U / mL aspartate endopeptidase, and 3.0 U / mL prions.

[0204] The positive control sample 56 was subjected to quality control testing according to the method described in Example 1, as shown in Table 16 and... Figure 13 This is the quality control test result for positive control sample 56.

[0205] Table 16

[0206]

[0207] As shown in Table 16, the positive control sample prepared in this comparative example does not contain the coagulation enzyme test, so the coagulation enzyme test does not develop color; and the prion concentration is too high, which inhibits the color development of glucuronidase, causing the test to fail.

[0208] Comparative Example 2:

[0209] Prepare positive control sample 57 by mixing the following components: pH 5.2, phosphate buffer 20mM, D-trehalose 10g / 100mL, L-amino acid oxidase 3U / mL, chitinase 10U / mL, phenylalanine aminopeptidase 20U / mL, xylan degrading enzyme 20U / mL, sialidase 10U / mL, and leukocyte esterase 15U / mL.

[0210] Positive control sample 57 was subjected to quality control testing and opening stability testing according to the method described in Example 1. Table 17 and Figure 14 This is the quality control test result for positive control sample 57.

[0211] Table 17

[0212]

[0213] As shown in Table 17, this comparative example does not include the coagulation enzyme and alkaline phosphatase items. Therefore, the above two items did not develop color, and the leukocyte esterase concentration was too high, which inhibited the color development of glucuronidase, causing the item to fail.

[0214] In summary, the applicant screened the types and concentrations of leukocyte esterase, N-acetylglucosidase, oxidase, coagulation enzyme, and alkaline phosphatase, and adjusted the concentration of bovine serum albumin to finally obtain the positive control formulation for this application. The positive control, used in conjunction with the negative control, enables simultaneous quality control of 11 items in vaginitis detection, significantly improving the poor stability of glucuronidase in traditional detection methods. Furthermore, the positive control exhibits excellent stability upon opening and long-term storage, making it highly suitable for widespread application.

[0215] The technical features of the above embodiments can be combined in any way. For the sake of brevity, not all possible combinations of the technical features in the above embodiments are described. However, as long as there is no contradiction in the combination of these technical features, they should be considered to be within the scope of this specification.

[0216] The embodiments described above are merely illustrative of several implementation methods of this application, and while the descriptions are specific and detailed, they should not be construed as limiting the scope of the invention patent. It should be noted that those skilled in the art can make various modifications and improvements without departing from the concept of this application, and these all fall within the protection scope of this application. Therefore, the protection scope of this application should be determined by the appended claims.

Claims

1. A quality control product for detecting vaginal secretions, characterized in that, Including negative control samples and positive control samples; The negative control, based on its total volume, comprises the following components: 20 mM to 200 mM basal buffer, 1% (w / v) to 5% (w / v) enzyme protectant, 0.05% (w / v) to 2% (w / v) lactate, 0.01% (w / v) to 5% (w / v) hydrogen peroxide, 0 U / mL to 0.005 U / mL leukocyte esterase, 0 to 0.01 U / mL sialidase, 0 to 0.04 U / mL N-acetylglucosidase, 0 to 45 U / mL oxidase, 0 to 1 U / mL coagulation enzyme, 0 to 40 U / mL β-glucuronidase, 0 to 4 U / mL proline aminopeptidase, and 0 to 0.8 U / mL alkaline phosphatase. The positive control, based on its total volume, comprises the following components: 20 mM–200 mM second basal buffer, 1% (w / v)–5% (w / v) second enzyme protectant, 0–0.04% (w / v) lactate, 0–0.005% (w / v) hydrogen peroxide, 0.01 U / mL–0.1 U / mL second leukocyte esterase assay, 0.02 U / mL–0.1 U / mL sialidase, and 0.05 U / m The following enzymes were tested: L~0.5U / mL second N-acetylglucosidase, 50U / mL~200U / mL second oxidase, 2U / mL~40U / mL second coagulation enzyme, 50U / mL~200U / mL β-glucuronidase, 5U / mL~20U / mL proline aminopeptidase, 1U / mL~5U / mL second alkaline phosphatase, and 0.2% (w / v)~1% (w / v) bovine serum albumin.

2. The quality control product for detecting vaginal secretions according to claim 1, characterized in that, At least one of the following conditions (1) to (4) must be met: (1) The first basic buffer and the second basic buffer are each independently selected from one or more of the following: citrate-sodium citrate buffer solution, acetic acid-sodium acetate buffer solution, disodium hydrogen phosphate-citric acid buffer solution and disodium hydrogen phosphate-sodium dihydrogen phosphate buffer solution; (2) The pH of the first basic buffer solution is 3.8 to 4.5; (3) The pH of the second basic buffer solution is 5.0–7.0; and (4) The first enzyme protectant and the second enzyme protectant are each independently selected from one or more of glycerol, D-sorbitol, mannitol, D-trehalose and sucrose.

3. The quality control product for detecting vaginal secretions according to claim 1, characterized in that, The first leukocyte esterase item and the second leukocyte esterase item are each independently selected from one or more of prions, porcine liver esterase, lipase, papain and acylated amino acid hydrolases.

4. The quality control product for detecting vaginal secretions according to claim 1, characterized in that, The first N-acetylglucosidase item and the second N-acetylglucosidase item are each independently selected from one or more of N-acetylglucosidase, cellulase, amylase, figase and acylated amino acid hydrolase.

5. The quality control product for detecting vaginal secretions according to claim 1, characterized in that, The first oxidase and the second oxidase are each independently selected from one or more of ascorbic acid oxidase and L-amino acid oxidase.

6. The quality control product for detecting vaginal secretions according to claim 1, characterized in that, The first coagulating enzyme and the second coagulating enzyme are each independently selected from one or more of trypsin, streptoprotein E, pectinase, amylase, and elastase.

7. The quality control product for detecting vaginal secretions according to claim 1, characterized in that, The first alkaline phosphatase item and the second alkaline phosphatase item are each independently selected from one or more alkaline phosphatases and acylated amino acid hydrolases.

8. The quality control product for detecting vaginal secretions according to any one of claims 1 to 7, characterized in that, Based on the total volume of the negative control product, the components of the negative control product further include: 0.01% (w / v) to 0.2% (w / v) of a first preservative; Optionally, the first preservative includes ProClin 300.

9. The quality control product for detecting vaginal secretions according to any one of claims 1 to 7, characterized in that, Based on the total volume of the positive control sample, the components of the positive control sample further include: 0.01% (w / v) to 0.2% (w / v) of a second preservative; Optionally, the second preservative includes ProClin 300.

10. A method for preparing a quality control sample for detecting vaginal secretions, characterized in that, Includes the following steps: Provide the components of the quality control product according to any one of claims 1 to 9, and prepare negative quality control products and positive quality control products respectively; The negative control and the positive control were vacuum dried to prepare lyophilized powder of positive control and lyophilized powder of negative control.

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