Beschreibung:
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.