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PMID: 410024 Published · ppublish English Journal Article

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 9 ·1977-09-00 ·Pages 3691-5

Hammarström S, Falardeau P

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.

MeSH Terms
Blood Platelets/enzymology Humans Kinetics Oxidoreductases/blood Prostaglandin Endoperoxides Prostaglandin-Endoperoxide Synthases/blood,isolation & purification Subcellular Fractions/enzymology Thromboxane-A Synthase/blood,isolation & purification
Chemicals
Prostaglandin Endoperoxides Oxidoreductases Prostaglandin-Endoperoxide Synthases Thromboxane-A Synthase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hammarström S
Falardeau P
References (20)
20 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.74.9.3691
Published
1977-09-00
Pages
3691-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431690
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.9.3691 PMC Full Text View journal details
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