Thromb Haemost 1984; 51(01): 016-021
DOI: 10.1055/s-0038-1660999
Original Article
Schattauer GmbH Stuttgart

Preparation and Characterization of NH2-Terminal Fibrinogen Bβ Fragments from N-DSK of Human Fibrinogen

Authors

  • S Birken

    The Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y., U.S.A.
  • G Agosto

    The Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y., U.S.A.
  • B Lahiri

    The Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y., U.S.A.
  • R Canfield

    The Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, N.Y., U.S.A.
Further Information

Publication History

Received 13 July 1983

Accepted 03 November 1983

Publication Date:
19 July 2018 (online)

Preview

Summary

In order to investigate the early release of NH2-terminal plasmic fragments from the Bβ chain of fibrinogen, substantial quantities of Bβ 1-42 and Bβ 1-21 are required as immunogens, as radioimmunoassay standards and for infusion into human volunteers to determine the half-lives of these peptides. Towards this end methods that employ selective proteolytic cleavage of these fragments from fibrinogen have been developed. Both the N-DSK fragment, produced by CNBr cleavage of fibrinogen, and Bβ 1-118 were employed as substrates for plasmin with the finding of higher yields from N-DSK. Bβ 1-42 and Bβ 1-21 were purified by gel filtration and ion-exchange chromatography on SP-Sephadex using volatile buffers. When the purified preparation of Bβ 1-42 was chromatographed on reverse-phase high performance liquid chromatography, two peaks of identical amino acid composition were separated, presumably due either to pyroglutamate or to amide differences.