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KMID : 0903519980410010047
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1998 Volume.41 No. 1 p.47 ~ p.52
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Characterization and Purification of a Microsomal 3-Hydroxy-3-Methylglutaryl-CoA Reductase in Rice Seedling
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김종범/Kim, Jong Bum
김종국/황영수/백융기/하선화/김제현/Kim, Jong Guk/Hwang, Young Soo/Paik, Young Ki/Ha, Sun Hwa/Kim, Jai Hyun
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Abstract
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3-Hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the conversion of HMG-CoA to mevalonic acid, the first intermediate of isoprenoid biosynthetic pathway in plants. The enzyme was solubilized with 0.4% Brij (polyoxyethylene ether) W-1 from a microsomal fraction of etiolated rice seedlings (Oryza sativa L.) in which its maximal activity was observed on the fourth day after germination. HMGR was purified to near homogeneity by employing (NH₄)₂SO₄ fractionation plus chromatographic procedures including DEAE-Sephadex A-50 and HMG-CoA-hexane-agarose affinity column. The size of the purified enzyme was estimated to be 55 kDa when judged by SDS-PAGE analysis with silver staining method. The apparent K_m and V_(max) values for HMG-CoA were determined to be 180 μM and 107 pmol/min/㎎, and those for NADPH were 810 μM and 32.1 pmol/min/㎎, respectively.
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