Solubilization and resolution of thromboxane synthesizing system from microsomes of bovine blood platelets.

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 fraction with prostaglandin H2 at lower temperature produced an unstable compound with platelet-aggregating activity, which was presumably thromboxane A2 and which decomposed readily to thromboxane B2 and 12L-hydroxy-5,8,10-heptadecatrienoic acid.

• Publication year

  1977

• Venue

  Journal of Biological Chemistry

• Publication date

  1977-08-25

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(17)40104-9PMID 885887
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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