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- W1988950957 abstract "Cathepsin G was used in vitro to digest human factor VII and factor IX. Clotting assays indicated that the proteinase affected a rapid loss in coagulant activity while in the presence of calcium ions the activity was almost totally protected. SDS-polyacrylamide gel electrophoresis indicated the removal of a peptide from each zymogen, VII-L from factor VII and IX-L from factor IX. This lead to the formation of VII-H and IX-H respectively. N-terminal analysis of the VII-H and IX-H products and COOH-terminal analysis of the VII-L and IX-L products confirmed that cathepsin G had cleaved position Phe40:Trp41 in factor VII and factor IX. The cleavage site is the same as that when cathepsin G is reacted with factor II, factor X and protein C. The unique action of cathepsin G may be part of a regulatory system for controlling the coagulant activity of vitamin K dependent clotting in vivo." @default.
- W1988950957 created "2016-06-24" @default.
- W1988950957 creator A5023604503 @default.
- W1988950957 date "1992-07-01" @default.
- W1988950957 modified "2023-09-27" @default.
- W1988950957 title "Cathepsin G, a regulator of human vitamin K, dependent clotting factors and inhibitors" @default.
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- W1988950957 doi "https://doi.org/10.1016/0049-3848(92)90134-v" @default.
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