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pubmed:abstractText |
The heavy chain of coagulation factor VII contains a serine esterase entity. A partial cleavage in the heavy chain occurs during purification and activation of the single-chain zymogen, presumably as a result of autolysis. Neutrophil cathepsin G initially generates a Gla-domainless FVIIa without coagulant activity. However, on extended exposure cleavage also occurs in the heavy chain, resulting in a complete loss of enzyme activity. Four cleavage sites on the heavy chain, two susceptible to trypsin-like autolysis and two susceptible to chymotrypsin-like cathepsin G-mediated catalysis have been identified. The hydrolysis of peptide bonds in the heavy chain might contribute to regulation of the coagulation process in vivo.
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