Abstract
In order to provide the basis for an investigation of fibrinogen metabolism through fibrinopeptide radioimmunoassay studies in an animal model, some structural features of canine fibrinogen have been elucidated. Canine fibrinogen and fibrin have been purified, their reduced, carboxymethylated chains separated, and their amino acid compositions and NH 2-terminal sequences determined. Canine fibrinogen was found to be very similar to human fibrinogen both in amino acid composition of the individual chains and in their NH 2-terminal amino acid sequences beyond the regions of fibrinopeptides A and B. The results confirm the structure of canine fibrinopeptides A and B by Blombäck et al. (1).
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