title: Proteolytic cleavage of human fibrinogen by cathepsin B.
abstract: Human fibrinogen was cleaved by human liver cathepsin B in vitro. The time course of the degradation was followed by SDS-PAGE. Using activated cathepsin B in a weight ratio of enzyme to fibrinogen of 1:100 a pH optimum of 6.0 was found at 37 degrees C. For the separation of the fibrinogen degradation products a reversed phase HPLC system was used. Fibrinogen was cleaved by cathepsin B at the C-terminal side of the A alpha-chain, partially also on its N-terminal side and at the N-terminal end of the B beta-chain.
authors.affiliation: Institut Jozef Stefan, Univerza E. Kardelja, Ljubljana, Jugoslavija.
authors.forename: D
authors.initials: D
authors.lastname: Gabrijelcic
authors.forename: R
authors.initials: R
authors.lastname: Gollwitzer
authors.forename: T
authors.initials: T
authors.lastname: Popović
authors.forename: V
authors.initials: V
authors.lastname: Turk
mesh_terms: D000911:Antibodies, Monoclonal; D002401:Cathepsin B / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000032:analysis*; D006801:Humans; D006868:Hydrolysis; D007118:Immunoassay; D010455:Peptides / Q000032:analysis
chemical_list: D000911:Antibodies, Monoclonal; D010455:Peptides; D005340:Fibrinogen; D002401:Cathepsin B