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- W2023588897 abstract "Cougulation factor VII contains ten λ‐carboxyglutamic acid residues in the N‐terminal region (Gla‐domain) which are essential for the hemostatic function of FVII. The present study shows that granulocyte cathepsin G degrades the Gla‐domain of FVIIa in vitro. Characterization of the truncated FVIIa by SDS‐PAGE and N‐terminal amino acid sequence analysis revealed that cleavage had occurred between Tyr‐44 and Ser‐45 and that further cleavage was only obtained on extensive cathepsin G exposure. Cleavage of vitamin K‐dependent coagulation factors by cathepsin G may play a role in vivo, and it offers a convenient way of obtaining proteins deprived of their Gla‐domain for functional and structural studies." @default.
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- W2023588897 date "1992-07-20" @default.
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- W2023588897 title "Generation of Gla-domainless FVIIa by cathepsin G-mediated cleavage" @default.
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- W2023588897 doi "https://doi.org/10.1016/0014-5793(92)80989-t" @default.
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