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Thromb Haemost 1981; 46(01): 240
DOI: 10.1055/s-0038-1652710
Fibrinogen – VII: Synthesis, Structure, Polymerization
Schattauer GmbH Stuttgart

Characterization Of A Crosslink-Containing Fragment Derived From The A Polymer Of Human Fibrin And Its Application In Immunologic Studies Using Monoclonal Antibodies

Authors

  • J H Sobel

    Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y. 10032

  • S Birken

    Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y. 10032

  • P Ehrlich

    Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y. 10032

  • R Friedman

    Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y. 10032

  • Z Moustafa

    Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y. 10032

  • R E Canfield

    Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y. 10032
Further Information

Publication History

Publication Date:
26 July 2018 (online)

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A high molecular weight crosslink-containing fragment derived from cyanogen bromide (CNBr) digests of the a polymer component of human fibrin has been isolated and characterized. The material has been used to generate monoclonal antibodies toward the goals of (1) producing fibrin-specific probes for use in the early detection of thrombosis and (2) generating monoclonal lines to single determinants in the COOH-terminal region of the Aα chain for use in structural studies of fibrinogen and fibrin.

Biochemical and immunologic characterization data indicate the fragment is comprised, predominantly, of equimolar quantities of the CNBr peptides spanning residues #241-476 (CNBr 8) and #518-584 (CNBr 10) in the original Aα chain. The acceptor and donor units are crosslinked via an average of 2.8-3.2 ε-(γ-glutamyl) lysine bonds per mole of CNBr 8 + CNBr 10 producing heterogeneously sized fragments in the range of 80,000-200,000 daltons.

Two types of monoclonal lines have been obtained. The first react with regions of primary structure and in one instance immunoreactivity could be localized to the Aa tryptic peptide #253-268. The second type appear to recognize conformational determinants as shown by one antibody that reacts well with the CNBr crosslinked fragment but poorly with its constituent peptides.