Isolation, characterization, and location of a donor-acceptor unit from cross-linked fibrin.
The cross-linking systems of bovine and human fibrins were studied by the introduction of a radioactive substitute donor as an inhibitor of fibrin cross-linking, separation of the constituent polypeptide chains after sulfitolysis, and tryptic digestion of the labeled gamma-chains. The information gathered from this approach enabled us to isolate and characterize the complete donor-acceptor unit in tryptic digests of fibrin gamma-gamma cross-linked systems. In both bovine and human fibrin, this kind of cross-linking is accomplished by reciprocal bridging between overlapping carboxy-terminal segments of neighboring gamma-chains. The amino acid sequence of the carboxy-terminal heptadecapeptide of the bovine gamma-chain was determined and an alignment of the corresponding region of the human gamma-chain established.
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D002417:Cattle; D002850:Chromatography, Gel; D004586:Electrophoresis; D005337:Fibrin / Q000302:isolation & purification*; D006801:Humans; D008722:Methods; D010455:Peptides / Q000032:analysis
D002247:Carbon Isotopes; D010455:Peptides; D005337:Fibrin