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The thromboxane synthetase system of the microsomes of bovine blood platelets was solubilized by the treatment with Triton X-100. The solubilized preparation was separated into two enzyme fractions by DEAE-cellulose chromatography. One catalyzed the formation of prostaglandin H2 from arachidonic acid in the presence of heme and tryptophan. The other fraction converted prostaglandin H2 to thromboxane B2 and 12L-hydroxy-5,8,10-heptadecatrienoic acid. However, incubation of the latter fractionpmid:885887 fatcat:bgyaasnf4jd35bc5uqibsh76m4