๐”– Bobbio Scriptorium
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Purification of prostaglandin H synthetase and a fluorometric assay for its activity

โœ Scribed by Alevtina T. Mevkh; Galina F. Sud'ina; Nikolay B. Golub; Sergey D. Varfolomeev

Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
535 KB
Volume
150
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

Prostaglandin H synthetase (PGH synthetase) has been purified to homogeneity from sheep vesicular glands. The pure enzyme has a specific activity of about 40 @.I of arachidonic acid consumed per minute per milligram of protein, which corresponds to a turnover number of 2800 mitt-' per subunit. The purified enzyme was obtained by one-sta8e chromatography on DEAE-Toyopearl 650 from Tween 20-solubihzed mictosomes. A sensitive fluorometric assay for PGH synthetase activity using homovanillic acid (HVA) as electron donor has been proposed. It has been shown that homovanilhc acid may be used as the electron donor and that in the presence of HVA the enzyme has an activity of -40 rM/miII/IIIg.

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