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. 1977 Sep;74(9):3691–3695. doi: 10.1073/pnas.74.9.3691

Resolution of prostaglandin endoperoxide synthase and thromboxane synthase of human platelets.

S Hammarström, P Falardeau
PMCID: PMC431690  PMID: 410024

Abstract

Thromboxane synthase was localized to the microsomes of human platelets. The enzyme was insensitive to sulfhydryl reagents and thiols but was inhibited by 12L-hydroperoxy-5, 8, 10, 14-eicosatetraenoic acid (concentration for 50% inhibition = 0.1 mM). Treatment of microsomes with Triton X-100 solubilized the enzymes that catalyze the conversion of arachidonic acid to thromboxane B2. The solubilized material was resolved by DEAE-cellulose chromatography into two components, one converting arachidonic acid to prostaglandins G2 and H2 and the other converting prostaglandin H2 to thromboxane B2.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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