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Hiroshi Ueno, Yasuo Bai, Edward J. Yatco, Nobuhiro Mori, Hiroyuki Kagamiyama, James M. Manning, Hemoglobin, a model protein for studying non-enzymatic glycation, Stem Cells, Volume 12, Issue S1, 1994, Pages 65–74, https://doi.org/10.1002/stem.5530120709
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Abstract
Non-enzymatic glycation of protein is a chemical modification reaction often found in human metabolism. Glycated hemoglobin (HbA1c) has been used as a model protein for studying non-enzymatic glycation because of its biological significance. Several questions have been raised in the course of studying this important biological reaction. Among them, we have focused on two major questions: 1) Why is the amino-terminus of the β-chain of human hemoglobin (HbA) a preferred target and not the amino-terminus of the α-chain, since HbA has Val residues in both its amino-termini? 2) Why do some Schiff base intermediates advance Amadori rearrangement but not others?
Since non-enzymatic glycation is a rather slow process, biochemical analysis is often difficult; a model system which mimics the chemistry of non-enzymatic glycation with a faster reaction rate has been developed. The model system using glycer-aldehyde with amino acids or peptides has demonstrated that the presence of a His-2(β) residue contributes significantly to the formation of HbA1c. Such a positively charged group is found at or near the glycation sites in many other non-enzymatically glycosylated proteins. Thus, it is feasible to assume a unique role for the positively charged residue in non-enzymatic glycation in general.
