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dc.contributor.authorRapepun Wititsuwannakulen_US
dc.contributor.authorDhirayos Wititsuwannakulen_US
dc.contributor.authorPlueng Suwanmaneeen_US
dc.contributor.otherPrince of Songkla Universityen_US
dc.contributor.otherMahidol Universityen_US
dc.identifier.citationPhytochemistry. Vol.29, No.5 (1990), 1401-1403en_US
dc.description.abstract3-Hydroxy-3-methylglutaryl coenzyme A reductase (mevalonate: NADP + oxidoreductase acylating CoA; EC was purified from fresh Hevea latex of clone RRIM 600. The latex was centrifuged and the sediment used for enzyme purification. The enzyme was solubilized by freeze-thawing in a buffer containing 1 % Brij W-1 and 20% glycerol. Affinity chromatography (HMG-CoA-Hexyl-Agarose) was used in the final purification step. The M r determined by SDS-PAGE was 44000 and that estimated from non-denaturing gel electrophoresis, 176000. The optimal pH was ca 7, with an apparent K m of 13 μM for (S)-HMG-CoA. A low concentration of dithiothreitol was required for maximal activity of the purified enzyme. © 1990.en_US
dc.rightsMahidol Universityen_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.title3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensisen_US
Appears in Collections:Scopus 1969-1990

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