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Method of pre-treating sample for measuring saccharified amine and method of measuring saccharified amine

a technology of saccharified amine and pre-treating sample, which is applied in the direction of enzymology, instruments, and detection of post translational modifications, can solve the problems of inability to perform reliable measurement and more hydrogen peroxide formation, and achieve the effect of eliminating influence and high accuracy

Active Publication Date: 2015-07-28
ARKRAY INC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

This approach enhances the accuracy of glycated amine measurements, reducing the influence of exogenous glycated amino acids and peptides, thereby improving the reliability of glycated hemoglobin as a diagnostic index in diabetes, allowing for consistent results regardless of the timing of blood collection.

Problems solved by technology

However, methods of measuring a glycated protein using such a redox reaction have a problem in that, for example, more hydrogen peroxide may be formed than is corresponding to the glycated protein actually contained in a sample.
Besides, depending on the patient, the measured value of a glycated protein may leap up temporarily, so that a reliable measurement cannot be performed.

Method used

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  • Method of pre-treating sample for measuring saccharified amine and method of measuring saccharified amine
  • Method of pre-treating sample for measuring saccharified amine and method of measuring saccharified amine

Examples

Experimental program
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Effect test

first embodiment

[0042]The present embodiment is one example of the first method, in which a FAOD-α is used to degrade the glycated amino acid and a FAOD-αS is used to measure the glycated protein.

[0043]First, whole blood is hemolyzed to prepare a hemolyzed sample. The method of causing the hemolysis is not particularly limited, and can be, for example, a method using a surfactant, a method using ultrasonic waves, a method utilizing a difference in osmotic pressure, and a method using a freeze-thawing technique. Among these, the method using a surfactant is preferable because of its simplicity in operation, etc.

[0044]As the surfactant, for example, non-ionic surfactants such as polyoxyethylene-p-t-octylphenyl ether (e.g. Triton series surfactants), polyoxyethylene sorbitan alkyl ester (e.g. Tween series surfactants), polyoxyethylene alkyl ether (e.g. Brij series surfactants), and the like can be used. Specific examples are products named Triton X-100, Tween-20, Brij 35, and the like. The conditions ...

second embodiment

[0064]The present embodiment is one example of the second method in which the same FAOD is used to degrade a glycated amino acid as a non-analyte glycation product and to measure a glycated protein as an analyte. The FAOD used in not particularly limited, and for example, any of a FAOD-α, a FAOD-S, and a FAOD-αS may be used.

[0065]A hemolyzed sample is prepared in the same manner as in the first embodiment, and a degradation FAOD is added to this hemolyzed sample.

[0066]The treatment is carried out, for example, under the conditions as follows: the concentration of the FAOD in the reaction solution in the range from 10 to 5000 U / l, the concentration of the blood cells in the reaction solution in the range from 0.5 to 20 vol %, the reaction temperature in the range from 20° C. to 50° C., the reaction period in the range from 1 minute to 1 hour, and the pH in the range from 6 to 9. This treatment usually is carried out in a buffer, and the same buffers as described above also can be use...

third embodiment

[0077]The present embodiment is an example where the same FAOD is used to degrade a glycated amino acid as a non-analyte glycation product and to measure a glycated protein as an analyte. However, the present embodiment differs from the above-described second embodiment in that it is not always necessary to inactivate a degradation FAOD with a protease. Because of the substrate specificity of enzymes, inactivating a FAOD with a protease can be difficult depending on the combination of the FAOD and protease. A method for measurement according to the present embodiment is effective in such a case. If a degradation FAOD added first reacts with a glycated protein degradation product formed by the treatment with a protease, the accuracy of the measurement cannot be improved. Accordingly, it is important to adjust the ratio of a degradation FAOD to a measurement FAOD added to a sample as described later.

[0078]First, a hemolyzed sample is prepared in the same manner as in the first embodim...

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Abstract

The present invention provides a method of pretreating a sample containing a glycated amine as an analyte, thereby enabling highly reliable measurement of a glycated amine. A glycated amino acid in the sample is degraded by causing a fructosyl amino acid oxidase (FAOD) to act thereon, and thereafter, a FAOD further is caused to act on the glycated amine as the analyte in the sample to cause a redox reaction. The amount of the glycated amine is determined by measuring the redox reaction. The substrate specificity of the FAOD caused to act on the glycated amino acid may be either the same as or different from that of the FAOD caused to act on the glycated amine. When using the same FAOD, a FAOD is caused to act on the glycated amino acid to degrade it, and thereafter, the sample is treated with a protease to inactivate the FAOD and also to degrade the glycated amine. Then, the same FAOD further is added so that the FAOD acts on the degradation product obtained to cause a redox reaction, and the redox reaction is measured.

Description

[0001]This application is a continuation reissue of U.S. patent application Ser. No. 13 / 653,024, filed on Oct. 16, 2012, now U.S. Pat. No. Re. 45,074, which is a continuation reissue of U.S. patent application Ser. No. 12 / 903,760, filed on Oct. 13, 2010, now U.S. Pat. No. Re. 43,795, which is a reissue of U.S. patent application Ser. No. 10 / 492,140, filed on Apr. 6, 2004, now U.S. Pat. No. 7,449,305, which is a 371 of PCT / JP02 / 10463, filed on Oct. 9, 2002, which claims foreign priority to Japanese Patent Application No. JP 2001-314218, filed on Oct. 11, 2001. TECHNICAL FIELD[0002]The present invention relates to a method of pretreating a sample for measurement of a glycated amine and to a method of measuring a glycated amine.BACKGROUND ART[0003]Conventionally, the measurement of the amount of an analyte in a sample using a redox reaction has been utilized for a wide range of applications. For example, such measurement has been utilized for measuring glycated amines (glycated protein...

Claims

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Application Information

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Patent Type & Authority Patents(United States)
IPC IPC(8): C12Q1/26C12Q1/37G01N33/68G01N33/00C12N9/06C12N9/52G01N33/72
CPCC12Q1/26G01N33/723G01N2333/906G01N2400/00G01N2440/38G01N2800/042C12N9/52C12Q1/37G01N33/68
Inventor YONEHARA, SATOSHIKOMORI, TSUGUKI
Owner ARKRAY INC
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