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Thrombospondin fragmentation by alpha-thrombin and resistance to gamma-thrombin.


ABSTRACT: In the presence of 2mM-Ca2+, alpha-thrombin slowly cleaved thrombospondin (Mr 180 000) into 150 000-Mr and 30 000-Mr fragments. In the absence of Ca2+, the platelet glycoprotein was progressively and completely hydrolysed by 3 units of the enzyme/ml to 130 000-Mr, 95 000-Mr and 65 000-Mr fragments. In contrast, the nonclotting enzyme form, gamma-thrombin, did not hydrolyse the platelet protein either in the presence or in the absence of Ca2+, even at 10-fold higher concentrations of enzyme. Protein-interacting regions removed from the catalytic site, like those required for fibrinogen recognition, are necessary for thrombin proteolysis of thrombospondin.

SUBMITTER: Takahashi K 

PROVIDER: S-EPMC1144480 | biostudies-other | 1984 Dec

REPOSITORIES: biostudies-other

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