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Updated: Apr 18, 2026

Biochemical Titration of Glycogen In vitro
Published on: November 24, 2013
Recent topics in chemical and clinical research on glycated albumin
Yuki Ueda1, Hideyuki Matsumoto2
1Diagnostics Department, Research and Development Group, Asahi Kasei Pharma Corporation, Shizuoka, Japan.
Abstract:
The measuring method for glycated albumin (GA) has been developed as a new glycemic control marker since the beginning of the 21st century. Since GA has an advantage in reflecting glycemic status over a shorter period than hemoglobin A1c (HbA1c), much research and many reviews have been reported. However, so far there have been few reports on glycation sites based on the tertiary structure of human serum albumin (HSA) and the comparison of glycation rates between GA and HbA1c in detail. The present review discusses how the glycation sites of lysine residues in HSA are modified with glucose, whereas the glycation sites of lysine residues are located inside of HSA as well as the direct comparison of glycation rates between GA and HbA1c using human blood. Moreover, the most recent clinical researches on GA are described.
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