Clinical Chemistry
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Clinical Chemistry 44: 256-263, 1998;
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(Clinical Chemistry. 1998;44:256-263.)
© 1998 American Association for Clinical Chemistry, Inc.

Endocrinology and Metabolism

Determination of glycated albumin by enzyme-linked boronate immunoassay (ELBIA)

Kazuyoshi Ikeda1, Yuichiro Sakamoto1, Yukie Kawasaki1, Takehiro Miyake2, Kimikazu Tanaka2, Takeyoshi Urata3, Yoshiaki Katayama4, Shoichi Ueda1, and Seikoh Horiuchi1,2

1 Department of Urology & Biochemistry, Kumamoto University School of Medicine, Honjo, 2-2-1, Kumamoto 860, Japan.

2 The Research Institute, Nacalai Tesque, Kyoto, Japan.

3 Department of Clinical Pathology, Showa University School of Medicine, Tokyo, Japan.

4 Laboratory of Clinical Chemistry, National Cardiovascular Center Hospital, Suita, Japan.

A new affinity method for quantification of glycated albumin by an enzyme-linked boronate-immunoassay (ELBIA) has been established, based on the interaction between boronic acids and the cis-diols of glycated human serum albumin (HSA) trapped by anti-HSA antibody. To evaluate the ELBIA, we first examined the accuracy of the conventional boronate affinity chromatographic (BAC) method. In the BAC method, 8.1–18.9% of nonglycated albumin calibrator nonspecifically bound to the boronate affinity column, values that were regarded as the column blank. In the modified BAC method, therefore, we subtracted the column blank value from the measured glycated albumin value to obtain the true value. Because 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.




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