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Purification of thromboxane synthetase and evidence of two distinct mechanisms for the formation of 12-L-hydroxy-5,8,10-heptadecatrienoic acid by porcine lung microsomes.

Authors
  • Hall, E R
  • Tai, H H
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Sep 24, 1981
Volume
665
Issue
3
Pages
498–503
Identifiers
PMID: 7197552
Source
Medline
License
Unknown

Abstract

Synthesis of thromboxane B2 and 12-L-hydroxy-5,8,10-heptadecatrienoic acid by crude microsomes and by partially purified thromboxane synthetase from porcine lung has been studied. Formation of both compounds catalyzed by the purified enzyme is inhibited similarly by imidazole or increased temperature (52 degrees C). However, during the initial stages of purification only the production of thromboxane B2 was diminished by imidazole or increased temperature, indicating the presence of an additional mechanism for the formation of 12-L-hydroxy-5,8,10-heptadecatrienoic acid. This novel mechanism is attributed to the effect of nondialyzable heat-stable factor(s) present in the crude preparation which stimulates the formation of 12-L-hydroxy-5,8,10-heptadecatrienoic acid from prostaglandin H2 in a time-dependent manner.

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