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18.97.9.172
18.97.9.172
SCIE
벼 HMG-CoA 환원효소의 특성연구
Characterization and Purification of a Microsomal 3-Hydroxy-3-Methylglutaryl-CoA Reductase in Rice Seedling
하선화 , 김제현 , 백융기 , 김종범 , 김종국 , 황영수 ( Sun Hwa Ha , Jai Hyun Kim , Young Ki Paik , Jong Bum Kim , Jong Guk Kim , Young Soo Hwang )
UCI I410-ECN-0102-2008-520-001467095

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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