Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

A stable reagent for the determination of aspartate aminotransferase

A technology of aspartate aminotransferase and reagents, which is applied in the field of biochemistry and clinical testing, and can solve problems such as reagent instability, difficulty in detecting serum AST, and accelerated stability experiments

Active Publication Date: 2022-03-11
BEIJING BEIJIAN XINCHUANGYUAN BIOLOGICAL TECH
View PDF7 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

This process also cannot avoid changes in temperature and humidity, and the sample is exposed to air after opening the cover, facing oxidation factors
Therefore, in this case, the accelerated stability test cannot evaluate the stability of other aspects (ISO standard 23640-2011, In vitro diagnostic medical devices-Evaluation of stability of in vitro diagnostic reagents)
[0012] At present, the double-reagent enzyme-coupled continuous detection method is mostly used in the market to detect serum AST. Due to the presence of enzyme and NADH in the reagent, the reagent is unstable during transportation and when the bottle cap is opened and operated on the machine. Serum AST poses difficulties

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • A stable reagent for the determination of aspartate aminotransferase
  • A stable reagent for the determination of aspartate aminotransferase
  • A stable reagent for the determination of aspartate aminotransferase

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0064] Embodiment 1: the preparation of comparison kit

[0065] First Reagent R1:

[0066]

[0067] Second reagent R2:

[0068] TRIS, pH6.5 100mmol / L

[0069] L-Aspartic Acid 720mmol / L

[0070] α-ketoglutarate 36mmol / L

Embodiment 2

[0071] Embodiment 2: the preparation of test kit

[0072] The preparation method of the second reagent R2 is the same as in Example 1; the preparation method of the first reagent R1 is shown in Table 1.

[0073] Table 1. R1 reagent composition of different test kits

[0074]

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The invention provides a stable reagent for measuring aspartate aminotransferase. The reagents of the present disclosure are dual reagents comprising TRIS, NADH, LDH, MDH, EDTA, Triton X-100, BSA, Proclin. The disclosed reagent can effectively improve the thermal stability, airborne stability and transportation stability of the NADH indicator system in vitro diagnostic reagent, and can effectively prolong the storage time of the kit.

Description

technical field [0001] This application relates to the fields of biochemistry and clinical testing. More specifically, the present application relates to a reagent for the determination of aspartate aminotransferase. Background technique [0002] There are two isoenzymes of aspartate aminotransferase (AST) in the liver, which exist in the mitochondria (mAST) and cytoplasm (sAST) of liver cells respectively. When the liver cells are mildly lesioned, only sAST is released into the blood; and when the lesion is severe, mAST is also released into the blood one after another. Therefore, serum AST activity increases with the degree of liver cell damage. [0003] In HBV-infected hepatitis and liver disease, AST increases slightly with ALT, or the amplitude is relatively large and the time is short, it may be mainly sAST, and the clinical significance is the same as ALT; AST increases more than ALT, although the amplitude is not too large The duration is very long, probably mainl...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(China)
IPC IPC(8): G01N21/31
CPCG01N21/31
Inventor 姜敏
Owner BEIJING BEIJIAN XINCHUANGYUAN BIOLOGICAL TECH
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com