AMINO-ACID SEQUENCES OF PORTIONS OF THE ALPHA-CHAIN AND BETA-CHAIN OF BOVINE FIBRINOGEN

The N-terminal portions of the Aα and Bβ chains of bovine fibrinogen (CNBr Aα and Bβ), each of which contains an ArgGly 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 GlyProArg 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. © 1979.