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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.date.accessioned2018-06-14T09:19:58Z-
dc.date.available2018-06-14T09:19:58Z-
dc.date.issued1990-01-01en_US
dc.identifier.citationPhytochemistry. Vol.29, No.5 (1990), 1401-1403en_US
dc.identifier.issn00319422en_US
dc.identifier.other2-s2.0-0011822416en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0011822416&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/15899-
dc.description.abstract3-Hydroxy-3-methylglutaryl coenzyme A reductase (mevalonate: NADP + oxidoreductase acylating CoA; EC 1.1.1.34) 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.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0011822416&origin=inwarden_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
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/0031-9422(90)80089-Yen_US
Appears in Collections:Scopus 1969-1990

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