PMID: 122295Apr 1, 1979

Nonenzymatic glycosylation of human hemoglobin at multiple sites

Metabolism: Clinical and Experimental
R ShapiroH F Bunn


The most abundant minor hemoglobin component of human hemolysate is Hb A1c, which has glucose bound to the N-terminus of the beta chain by a ketoamine linkage. Hb A1c is formed slowly and continuously throughout the 120 day lifespan of the red cell. It can be synthesized in vitro by incubating purified hemoglobin with 14C-glucose. Other minor components, Hb A1a1 and Hb A1a2 are adducts of sugar phosphates at the N-terminus of the beta chain. Hb A1b contains an unidentified nonphosphorylated sugar at the beta N-terminus. In addition, a significant portion of the major hemoglobin component (Hb Ao) is also glycosylated by a glucose ketoamine linkage at other sites on the molecule, including the N-terminus of the alpha chain and the epsilon-amino group of several lysine residues on both the alpha and the beta chains. The results indicate that the interaction of glucose and hemoglobin is rather nonspecific and suggests that other proteins are modified in a similar fashion.


Dec 1, 1983·Scandinavian Journal of Clinical and Laboratory Investigation·S WettreH von Schenck
Sep 21, 2012·Clinical Chemistry and Laboratory Medicine : CCLM·Philippe Gillery
Jul 1, 1982·Indian Journal of Pediatrics·S C Kalhan
Jan 1, 1981·Journal of Endocrinological Investigation·M TrovatiG Lenti
Oct 1, 2015·Archives of Endocrinology and Metabolism·Sailaja AnantarapuDharaneswari Vemvakam
Nov 4, 2017·Critical Reviews in Biochemistry and Molecular Biology·Kerryanne CrawfordIvan Ahel
Feb 19, 2015·Journal of Diabetes Science and Technology·Eric P Smith, Robert M Cohen
Aug 5, 2017·Sensors·Hua Lin, Jun Yi

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In Vitro [Publication Type]

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