Kinetic studies on the conversion of prostaglandin endoperoxide PGH2 by thromboxane synthase. Prostaglandins 1978 Oct;16(4):563-70
Date
10/01/1978Pubmed ID
725086DOI
10.1016/0090-6980(78)90186-7Scopus ID
2-s2.0-0018088987 (requires institutional sign-in at Scopus site) 23 CitationsAbstract
We have investigated the time course of formation of thromboxane A2, thromboxane B2, and the C-17 hydroxy fatty acid, HHT, from arachidonic acid in a washed human platelet suspension. Our results indicate that HHT is not a breakdown product of thromboxane A2, but rather thromboxane A2 decomposes exclusively into thromboxane B2. The kinetics of formation of thromboxane B2 from the endoperoxide prostaglandin H2 in human platelet microsomes was examined. Our data suggest that a bimolecular reaction is involved in the formation of thromboxane A2 from prostaglandin H2 and that thromboxane synthase is not an isomerase, but may be acting via a dismutase-type reaction. One possibility is that thromboxane and HHT are produced simultaneously from two molecules of prostaglandin H2.
Author List
Anderson MW, Crutchley DJ, Tainer BE, Eling TEMESH terms used to index this publication - Major topics in bold
Arachidonic AcidsBlood Platelets
Fatty Acids
Humans
Microsomes
Oxidoreductases
Prostaglandin Endoperoxides
Prostaglandins H
Thromboxane A2
Thromboxane B2
Thromboxane-A Synthase
