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Proteolytic cleavage of human fibrinogen by cathepsin B
D Gabrijelcic1, R Gollwitzer, T Popović
1Institut Jozef Stefan, Univerza E. Kardelja, Ljubljana, Jugoslavija.
Biological Chemistry Hoppe-Seyler
|May 1, 1988
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.