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. 1985 Feb;28(2):87-9.
doi: 10.1007/BF00279921.

Glycosylation of human fibrinogen in vivo

A Lütjens, A A te Velde, E A vd Veen, J vd Meer

Glycosylation of human fibrinogen in vivo

A Lütjens et al. Diabetologia. 1985 Feb.

Abstract

Fibrinogen was purified from plasma from 22 non-diabetic and 26 poorly controlled Type 1 (insulin-dependent) diabetic subjects. In non-diabetic subjects, 0.95 +/- 0.17 mol glucose was bound per mol fibrinogen, whereas in the diabetic subjects 1.33 +/- 0.21 mol glucose was bound per mol fibrinogen (mean +/- SD, p less than 0.001). Comparison of the amount of bound glucose, when estimated by two different methods, suggested that lysine is the site of glycosylation. It is currently unknown whether this increased glycosylation of fibrinogen alters its function.

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