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

Degradation Pathway of Fibrinogen by Plasmin

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

Publication Date:
04 July 2018 (online)

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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.

* Present address: Department of Internal Medicine, School of Medicine and Dentistry, University of Rochester, Rochester, N. Y. 14642


 

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