Method for measuring glycosylated hemoglobin, and device for measuring glycosylated hemoglobin

A technology of glycosylated hemoglobin and hemoglobin, applied in the field of glycosylated hemoglobin, which can solve problems such as difficult to reflect symptoms

Active Publication Date: 2018-12-21
TOSOH CORP
View PDF2 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Furthermore, it has been reported in recent years (Non-Patent Documents 1 to 3) that, although rare, blood samples to be measured for glycosylated hemoglobin contain various abnormal hemoglobins produced as a result of the above-mentioned gene mutations. In the chromatographic measurement method, measurement results reflecting

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
  • Method for measuring glycosylated hemoglobin, and device for measuring glycosylated hemoglobin
  • Method for measuring glycosylated hemoglobin, and device for measuring glycosylated hemoglobin
  • Method for measuring glycosylated hemoglobin, and device for measuring glycosylated hemoglobin

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0111] For blood samples containing abnormal hemoglobin D, the following method of the present invention was implemented: in the chromatogram obtained by cation exchange chromatography ( Figure 5 ), calculate the total peak area (Total area) of the chromatogram and the peak areas of A1a, A1b, HbF, LA1c, sA1c, A', H-V0, and obtain the X1c area according to the formula (3), according to the formula ( 2) Determine the area of ​​A0, and calculate A1c% according to formula (1). It should be noted that the peak detection range of H-V0 is 1.00±0.07 minutes.

[0112] (1) Peak area of ​​A'

[0113] Calculate the peak area of ​​A' according to the chromatogram to be 921.2.

[0114] (2) Peak area of ​​α

[0115] According to the chromatogram, the peak area of ​​α was calculated to be 8.0+6.7+38.1+63.9=116.7.

[0116] (3) Peak area of ​​sA1c

[0117] According to the chromatogram, the peak area of ​​sA1c was calculated to be 63.9.

[0118] (4) Peak area of ​​X0

[0119] Calculate t...

Embodiment 2

[0131] For blood samples containing abnormal hemoglobin S, the following method of the present invention was implemented: in the chromatogram obtained by cation exchange chromatography ( Image 6 ), calculate the total peak area (Total area) of the chromatogram and each peak area of ​​A1a, A1b, HbF, LA1c, sA1c, A', H-V1, and obtain the X1c area according to the formula (3), according to the formula ( 2) Determine the area of ​​A0, and calculate A1c% according to formula (1). It should be noted that the peak detection range of H-V1 is 1.16±0.09 minutes.

[0132] (1) Peak area of ​​A'

[0133] Calculate the peak area of ​​A' according to the chromatogram to be 899.0.

[0134] (2) Peak area of ​​α

[0135] According to the chromatogram, the peak area of ​​α was calculated to be 11.8+7.8+31.4+78.6=129.6.

[0136] (3) Peak area of ​​sA1c

[0137] According to the chromatogram, the peak area of ​​sA1c was calculated to be 78.6.

[0138] (4) Peak area of ​​X0

[0139] Calculat...

Embodiment 3

[0151] For blood samples containing abnormal hemoglobin C, the following method of the present invention was implemented: in the chromatogram obtained by cation exchange chromatography ( Figure 7 ), calculate the peak areas of A1a, A1b, LA1c, sA1c, and A0, and calculate A1c% according to formula (4). It should be noted that the peak detection range of H-V2 is 1.34±0.09 minutes.

[0152] (1) Peak area of ​​A0

[0153] According to the chromatogram, the peak area of ​​A0 was calculated to be 1140.3.

[0154] (2) Peak area of ​​α

[0155] According to the chromatogram, the peak area of ​​α was calculated to be 10.8+11.8+34.8+89.9=147.3.

[0156] (3) Peak area of ​​sA1c

[0157] According to the chromatogram, the peak area of ​​sA1c was calculated to be 89.9.

[0158] (8) Calculation of A1c%

[0159] Substituting the numerical value obtained above into formula (4), A1c%=6.7% was calculated.

[0160] (9) Converted to NGSP value (conversion factors 1.1151, 0.6558)

[0161] ...

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 purpose of the present invention is to eliminate the effect of abnormal hemoglobin when a blood sample containing abnormal hemoglobin D, abnormal hemoglobin S, or abnormal hemoglobin C is measuredby cation exchange chromatography, and to obtain an sA1c measurement result reflecting a symptom of the test subject providing the blood sample. The abovementioned problem is solved by a method for measuring the ratio (%) of sA1c, characterized by comprising calculating the area of the peak when a peak originating from abnormal hemoglobin D, abnormal hemoglobin S, or abnormal hemoglobin C is identified and measuring the ratio (%) of sA1c corrected using the calculation result.

Description

technical field [0001] The present invention relates to a method and device for measuring glycated hemoglobin in a blood sample by liquid chromatography, and more particularly to a glycated hemoglobin capable of measuring glycated hemoglobin as a diagnostic index for diabetes in a blood sample group in which blood samples containing abnormal hemoglobin may be mixed measuring method and measuring device. Background technique [0002] Hemoglobin has an α2β2 structure consisting of 2 α chains and 2 β chains. In addition to hemoglobin A, which accounts for about 97% of the total hemoglobin, it is composed of hemoglobin F and hemoglobin A2. The hemoglobin F has 2 α chains and 2 The α2γ2 structure composed of γ chains accounts for less than 1% of the total hemoglobin, and the hemoglobin A2 has an α2δ2 structure composed of two α chains and two δ chains and accounts for less than 1% of the total hemoglobin. [0003] Hemoglobin non-enzymatically combines with sugar (blood sugar) pr...

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
IPC IPC(8): G01N30/88G01N30/02G01N30/86G01N33/49
CPCG01N2030/8822G01N30/8679G01N30/88B01D15/362G01N33/49G01N30/02G01N30/86G01N33/723G01N30/8631G01N30/8637
Inventor 长谷川幸行
Owner TOSOH CORP
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products