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. 1986 Feb 1;233(3):637–641. doi: 10.1042/bj2330637

Production of platelet thromboxane A2 inactivates purified human platelet thromboxane synthase.

E R Hall, W M Tuan, D L Venton
PMCID: PMC1153079  PMID: 3707514

Abstract

Human platelet thromboxane synthase was partially purified by DEAE-cellulose, Affi-Gel Blue, and Sephacryl S-300 chromatography to a specific activity of 259 nmol of thromboxane B2/min per mg. Thromboxane synthase retained 75-90% of its enzymic activity when bound to phenyl-Sepharose. The immobilized enzyme was inactivated at pH 3.0 and inhibited by 1-benzylimidazole and U-63,557A. The ability of the enzyme to produce thromboxane A2 from prostaglandin H2 was dramatically reduced by multiple additions of prostaglandin H2. Our data suggest that the production of thromboxane A2 by the enzyme is self-limiting and that the enzyme is inactivated during the reaction.

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Selected References

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