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• W956048083 abstract "The term glycohemoglobin (glycated hemoglobin) refers to hemoglobin that has been modified postribosomally by the attachment of glucose to the polypeptide chain. This modification, generically designated nonenzymatic glycation, is a condensation reaction between the carbohydrate and a free amino group at the amino terminus or ɛ-amino group of a lysine residue. The study of hemoglobin glycation has served as a model system; for it is now clear that many proteins undergo nonenzymatic glycation. The reaction is initiated with attachment of acyclic glucose to a protein amino group via nucleophilic addition, forming an aldimine, also known as a Schiff base. This intermediate product subsequently undergoes an Amadori rearrangement to form a 1-amino-1-deoxyfructose derivative in stable ketoamine linkage. The reaction is slow and continuous, and the extent of glycation is largely dependent on the glucose concentration to which the protein is exposed during its lifetime in the circulation. Other factors that influence the sites and amount of glycation include the accessibility and pKa of the amino groups within the structure of the protein." @default.
• W956048083 created "2016-06-24" @default.
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• W956048083 date "1994-01-01" @default.
• W956048083 modified "2023-09-24" @default.
• W956048083 title "[5] Purification of glycated hemoglobin" @default.
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• W956048083 doi "https://doi.org/10.1016/0076-6879(94)31007-6" @default.
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