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Artigo Revisado por pares
BIBTEX RIS

Amino acid sequences of portions of the α and β chains of bovine fibrinogen

1979; Elsevier BV; Volume: 192; Issue: 1 Linguagem: Inglês

10.1016/0003-9861(79)90068-7

ISSN

1096-0384

Autores

Richard A. Martinelli, A.S. Inglis, Michael R. Rubira, Thomas C. Hageman, John G.R. Hurrell, Sydney Leach, Harold A. Scheraga,

Tópico(s)

Iron Metabolism and Disorders

Resumo

The N-terminal portions of the Aα and Bβ chains of bovine fibrinogen (CNBr Aα and Bβ), each of which contains an ArgGly bond that is hydrolyzed by thrombin, have been isolated by cyanogen bromide cleavage of fibrinogen and column chromatography of the resulting material. These peptides were digested with thrombin, releasing fibrinopeptide A and GlyProArg from CNBr Aα, and fibrinopeptide B from CNBr Bβ. The C-terminal peptides produced by digestion with thrombin (CNBr α and CNBr β) were purified, and the amino acid sequences of portions of these peptides (30 residues from the N-terminus of CNBr α and 32 residues from the N-terminus of CNBr β) were determined with an automatic sequenator using the Edman degradation.

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