Determination of serum glycated albumin by high-performance affinity chromatography.

Abstract

Serum albumin has a shorter half-life than hemoglobin. Masurement of glycated albumin (GA) therefore provides useful information on short-term blood glucose control in diabetic patients. We developed and evaluated a rapid and simple method for determination of GA. Glycated and non-glycated proteins were separated by high-performance affinity chromatography on immobilized boronate. Albumin in both fractions was detected by postcolumn reaction with Bromocresol Purple. GA could analyzed rapidly (4 min) without pretreatment such as separation of albumin from other serum proteins. The effect of chromatographic conditions on the amount of GA was studied. The amount of GA was dependent on separation time, eluent composition, pH and separation temperature. It is therefore necessary to control thoroughly the chromatographic conditions. However, the reproducibility was quite satisfactory under controlled conditions (RSD, 1.09~3.04). Therefore, the method should be useful for routine analysis of GA. © 1992, The Japan Society for Analytical Chemistry. All rights reserved.