, Volume 28, Issue 2, pp 87–89 | Cite as

Glycosylation of human fibrinogen in vivo

  • A. Lütjens
  • A. A. te Velde
  • E. A. v. d. Veen
  • J. v. d. Meer


Fibrinogen was purified from plasma from 22 nondiabetic 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<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.

Key words

Fibrinogen glycosylation Type 1 diabetes 


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Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • A. Lütjens
    • 1
  • A. A. te Velde
    • 2
  • E. A. v. d. Veen
    • 2
  • J. v. d. Meer
    • 2
  1. 1.Department of Clinical ChemistryAndreas HospitalThe Netherlands
  2. 2.Department of Internal MedicineFree University HospitalAmsterdamThe Netherlands

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