DETERMINATION OF GLYCATED ALBUMIN BY ENZYME-LINKED BORONATE IMMUNOASSAY (ELBIA)

Citation
K. Ikeda et al., DETERMINATION OF GLYCATED ALBUMIN BY ENZYME-LINKED BORONATE IMMUNOASSAY (ELBIA), Clinical chemistry, 44(2), 1998, pp. 256-263
Citations number
21
Categorie Soggetti
Medical Laboratory Technology
Journal title
ISSN journal
00099147
Volume
44
Issue
2
Year of publication
1998
Pages
256 - 263
Database
ISI
SICI code
0009-9147(1998)44:2<256:DOGABE>2.0.ZU;2-1
Abstract
A new affinity method for quantification of glycated albumin by an enz yme-linked boronate-immunoassay (ELBIA) has been established, based on the interaction between boronic acids and the cis-diols of glycated h uman serum albumin (HSA) trapped by anti-HSA antibody. To evaluate the ELBIA, we first examined the accuracy of the conventional boronate af finity chromatographic (BAC) method. In the BAC method, 8.1-18.9% of n onglycated albumin calibrator nonspecifically bound to the boronate af finity column, values that were regarded as the column blank. In the m odified BAC method, therefore, we subtracted the column blank value fr om the measured glycated albumin value to obtain the true value. Becau se glycated albumin values measured by ELBIA were exactly the same as reported by the modified BAC method, we suggest that the ELBIA results reflect the real status of albumin glycation. We have also developed a fully automated ELBIA system, allowing multiple, rapid, and precise measurements of glycated albumin.