Amino acid sequence studies on the α chain of human fibrinogen. Location of four plasmin attack points and a covalent cross-linking site

Abstract

The amino acid sequence of a 38-residue midsection piece of the alpha chain of human fibrinogen has been determined using a combination of plasmin-derived peptides and cyanogen bromide fragments. The segment contains several important features, including four early plasmin attack points, one of the two alpha-chain cross-linking acceptor sites, and a peptide homologous to one isolated from plasmin digests of bovine fibrinogen, and reported to have anticoagulant activity. The segment is sequentially adjacent to and overlapping with a large molecular weight (20000-25000) fragment released during plasminolysis. This latter material is very rich in glycine and serine and deficient in nonpolar amino acids. It also contains the other alpha-chain cross-linking acceptor site.