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Clinical Chemistry 33: 2220-2224, 1987;
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Clinical Chemistry, Vol 33, 2220-2224, Copyright © 1987 by American Association for Clinical Chemistry

Non-enzymic glycation of individual plasma proteins in normoglycemic and hyperglycemic patients

GE Austin, RH Mullins and LG Morin
Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322.

Diabetic patients in poor glycemic control show increased glycation of total plasma proteins, but little is yet known about the relative extents to which the various individual proteins are glycated. Thus, we studied the non-enzymic glycation of several major plasma proteins and plasma protein fractions in normal and diabetic patients. In vivo glycation for most plasma proteins was very low in non-diabetic patients, only gamma globulin showing more than 5% glycation. In diabetic plasmas, glycation was much greater, immunoglobulins again showing the greatest proportion, followed in descending order by albumin, complement C3, fibrinogen, transferrin, haptoglobin, and alpha- 1-antitrypsin. When plasma proteins were glycated in vitro, this order was IgG greater than complement C3 greater than albumin greater than transferrin greater than haptoglobin greater than alpha-1-antitrypsin. In general, proteins with the longest biological half-lives, such as IgG and albumin, showed the greatest in vivo glycation. On the other hand, proteins with high intrinsic glycability, such as complement C3, showed moderate glycation, despite a short half-life. Except for albumin, more basic proteins showed greater glycation than acidic proteins, but there was poor correlation between mole percent lysine and glycation. Evidently the relative extents of glycation of different plasma proteins are a complex function of integrated glucose concentrations over time and of the half-life and chemical characteristics of each protein.


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Copyright © 1987 by the American Association for Clinical Chemistry.