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Cited by 876

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

The Glycosylation of Hemoglobin: Relevance to Diabetes Mellitus

Bunn, H. Franklin, Gabbay, Kenneth H., Gallop, Paul M.·1978·Science

Abstract

Glucose reacts nonenzymatically with the NH 2 -terminal amino acid of the β chain of human hemoglobin by way of a ketoamine linkage, resulting in the formation of hemoglobin A Ic . 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 A Ic in the red cells of patients with diabetes mellitus. By providing an integrated measurement of blood glucose, hemoglobin A Ic 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.

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Crossref · 10.1126/science.635569

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Metadata

Authors
Bunn, H. F., Gabbay, K. H., & Gallop, P. M.
Venue
Science
Published
1978-04-07
Volume
200
Issue
4337
Pages
21-27
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2073620575
Cited by
876
References
2
FWCI
48.96
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: The Glycosylation of Hemoglobin: Relevance to Diabetes Mellitus. https://app.cochat.ai/papers/10.1126/science.635569
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Bunn, H. F., Gabbay, K. H., & Gallop, P. M. (1978). The Glycosylation of Hemoglobin: Relevance to Diabetes Mellitus. Science. https://doi.org/10.1126/science.635569

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.