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

Research output: Contribution to journal › Article › Academic › peer-review

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

Original language	English
Pages (from-to)	87-89
Journal	Diabetologia
Volume	28
Issue number	2
Publication status	Published - 1985

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title = "Glycosylation of human fibrinogen in vivo",

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",

author = "A. L{\"u}tjens and \{te Velde\}, \{A. A.\} and \{vd Veen\}, \{E. A.\} and \{vd Meer\}, J.",

year = "1985",

language = "English",

volume = "28",

pages = "87--89",

journal = "Diabetologia",

issn = "0012-186X",

publisher = "Springer Verlag",

number = "2",

}

TY - JOUR

T1 - Glycosylation of human fibrinogen in vivo

AU - Lütjens, A.

AU - te Velde, A. A.

AU - vd Veen, E. A.

AU - vd Meer, J.

PY - 1985

Y1 - 1985

N2 - 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

AB - 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

M3 - Article

C2 - 3920098

SN - 0012-186X

VL - 28

SP - 87

EP - 89

JO - Diabetologia

JF - Diabetologia

IS - 2

ER -

Glycosylation of human fibrinogen in vivo

Abstract

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