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The proteolytic action of ancrod on human fibrinogen and its polypeptide chains

1973; Elsevier BV; Volume: 2; Issue: 1 Linguagem: Inglês

10.1016/0049-3848(73)90082-0

1879-2472

W. Edgar, C. R. M. Prentice,

Polysaccharides Composition and Applications

The digestion of human fibrinogen and fibrin by the coagulant enzyme ancrod (Arvin) was studied, and by use of polyacrylamide gel electrophoresis in sodium dodecyl sulphate (SDS) the molecular weights of subunit polypeptides and digestion products were estimated. Ancrod attacked only the α (A) chain of human fibrinogen to produce a polypeptide of molecular weight 39,000 which was bound within the clot, and also a free polypeptide of 31,000 which appeared in the supernatant and was further digested to fragments of 27,000, 25,000, 16,000 and about 10,000. Ancrod in higher concentrations also digested the α polymers of crosslinked fibrin producing fragments similar to those from the α (A) monomer but differing in their distribution between clot and supernatant. Digestion of the separated α (A), β (B) and γ chains of S-carboxymethyl fibrinogen by ancrod showed the α (A) chain to be the most susceptible to proteolysis and that the same digestion products were formed as from the intact fibrinogen molecule. Additionally, limited proteolytic digestion of the separated γ chain was observed.