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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

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.
› Author Affiliations
Further Information

Publication History

Received 13 July 1983

Accepted 03 November 1983

Publication Date:
19 July 2018 (online)

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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.

Key Words

Fibrin degradation products - Plasmin - Fibrinogen
 

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