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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-04-07
    Description: Glucose reacts nonenzymatically with the NH2-terminal amino acid of the beta chain of human hemoglobin by way of a ketoamine linkage, resulting in the formation of hemoglobin AIc. Other minor components appear to be adducts of glucose 6-phosphate and fructose 1,6-diphosphate. These hemoglobins are formed slowly and continuously throughout the 120-day life-span of the red cell. There is a two- to threefold increase in hemoglobin AIc in the red cells of patients with diabetes mellitus. By providing an integrated measurement of blood glucose, hemoglobin AIc is useful in assessing the degree of diabetic control. Furthermore, this hemoglobin is a useful model of nonenzymatic glycosylation of other proteins that may be involved in the long-term complications of the disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bunn, H F -- Gabbay, K H -- Gallop, P M -- New York, N.Y. -- Science. 1978 Apr 7;200(4337):21-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/635569" target="_blank"〉PubMed〈/a〉
    Keywords: Blood Glucose/metabolism ; Chemical Phenomena ; Chemistry ; Diabetes Complications ; Diabetes Mellitus/*blood/diagnosis ; Diphosphoglyceric Acids/blood ; Glycosides/blood ; Glycosuria/etiology ; Hemoglobin A/*metabolism ; Hemoglobins/*analysis/*metabolism ; Humans ; Kinetics ; Oxygen/blood ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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