Wilson T M, Russell D W
Department of Biochemistry, University of Otago, Dunedin, New Zealand.
Biochem Biophys Res Commun. 1992 Apr 15;184(1):530-7. doi: 10.1016/0006-291x(92)91227-h.
HMG-CoA reductase was located to the envelope membranes of pea etioplasts, the first report of the suborganelle localization of this key enzyme in isoprenoid synthesis. The enzyme was purified 156 fold from isolated envelope membranes. Purification was achieved by detergent solubilization, hydroxylapatite chromatography and glycerol gradient centrifugation. Membrane-bound etioplast HMG-CoA reductase was activated 4 to 5 fold by high concentrations of inorganic phosphate, this activation was prevented by arsenate, a structural analog of phosphate.
HMG-CoA还原酶定位于豌豆黄化质体的包膜膜上，这是该类异戊二烯合成关键酶在亚细胞器定位方面的首次报道。该酶从分离的包膜膜中纯化了156倍。通过去污剂增溶、羟基磷灰石层析和甘油梯度离心实现了纯化。膜结合的黄化质体HMG-CoA还原酶被高浓度无机磷酸盐激活4至5倍，这种激活被磷酸盐的结构类似物砷酸盐所抑制。
