3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis
3-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 cont...
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th-mahidol.158992020-07-08T12:54:54Z 3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis Rapepun Wititsuwannakul Dhirayos Wititsuwannakul Plueng Suwanmanee Prince of Songkla University Mahidol University Agricultural and Biological Sciences Biochemistry, Genetics and Molecular Biology 3-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. 2018-06-14T09:19:58Z 2018-06-14T09:19:58Z 1990-01-01 Article Phytochemistry. Vol.29, No.5 (1990), 1401-1403 10.1016/0031-9422(90)80089-Y 00319422 2-s2.0-0011822416 https://repository.li.mahidol.ac.th/handle/123456789/15899 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0011822416&origin=inward |
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Agricultural and Biological Sciences Biochemistry, Genetics and Molecular Biology Rapepun Wititsuwannakul Dhirayos Wititsuwannakul Plueng Suwanmanee 3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis |
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3-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. |
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Prince of Songkla University |
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Prince of Songkla University Rapepun Wititsuwannakul Dhirayos Wititsuwannakul Plueng Suwanmanee |
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Rapepun Wititsuwannakul Dhirayos Wititsuwannakul Plueng Suwanmanee |
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Rapepun Wititsuwannakul |
title |
3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis |
title_short |
3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis |
title_full |
3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis |
title_fullStr |
3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis |
title_full_unstemmed |
3-Hydroxy-3-methylglutaryl coenzyme a reductase from the latex of Hevea brasiliensis |
title_sort |
3-hydroxy-3-methylglutaryl coenzyme a reductase from the latex of hevea brasiliensis |
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2018 |
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https://repository.li.mahidol.ac.th/handle/123456789/15899 |
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1763495835833729024 |