Summary
Human pro-coagulant α-thrombin may be proteolyzed under controlled conditions to the non-coagulant β- and γ-thrombin forms. These derivative forms nonetheless retain esterase and amidase activities with small substrates as well as several other thrombin functions. Structurally, human γ-thrombin consists of three non-covalently associated fragments which retain structural integrity as measured by several spectroscopic criteria as well as enzymatic function. The protein folding characteristics of three-chain γ-thrombin indicate that each fragment (domain) contains sufficient information to result in a correct renaturation of protein conformation. Those subtle structural differences which distinguish γ- from α-thrombin are most likely the obstructions to fibrinogen binding which account for the loss of clotting activity.
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Berliner, L.J. Structure-function relationships in human α- and γ-thrombins. Mol Cell Biochem 61, 159–172 (1984). https://doi.org/10.1007/BF00222493
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DOI: https://doi.org/10.1007/BF00222493