Degradation Pathway of Fibrinogen by Plasmin

Andrei Z. Budzynski; Victor J. Marder

doi:10.1055/s-0038-1651898

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1977; 38(04): 0793-0800
DOI: 10.1055/s-0038-1651898

Original Article

Schattauer GmbH

Degradation Pathway of Fibrinogen by Plasmin

Autor*innen

Andrei Z. Budzynski

¹Departments of Medicine and Biochemistry and the Specialized Center of Research in Thrombosis, Temple University Health Sciences Center, Philadelphia, Pennsylvania, 19140, U.S.A.
Victor J. Marder^*

¹Departments of Medicine and Biochemistry and the Specialized Center of Research in Thrombosis, Temple University Health Sciences Center, Philadelphia, Pennsylvania, 19140, U.S.A.

Abstract

Summary

The molecular weights of derivatives obtained from chemical and enzymatic degradation of fibrinogen and fibrin support a model in which the two halves of the fibrinogen molecule are covalently linked by a set of disulfide bonds at the amino-terminal region. The 2 asymmetric cleavages caused by plasmin in the fibrinogen molecule occur according to the reactions:

X → Y + D

Y → E + D

The quantitative analysis of the amino-terminal amino acids in fragments D (from fibrinogen) and DD (from crosslinked fibrin) yields a total of 3.0 and 6.9 moles of amino acids per mole of protein, indicating three and six polypeptide chain structures, respectively. The data on molecular weights, polypeptide chain composition and immunologic properties of fibrinogen degradation products support the hypothesis on the asymmetric pathway of fibrinogen degradation by plasmin and the formation of two fragment D and one fragment E molecules from each molecule of fibrinogen.

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Referenzen

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