Parker R A, Miller S J, Gibson D M
Biochem Biophys Res Commun. 1984 Dec 14;125(2):629-35. doi: 10.1016/0006-291x(84)90585-0.
Conversion of native, 97-100 kDa rat liver microsomal HMG CoA reductase to membrane-bound 62 kDa and soluble 52-56 kDa catalytically active forms was catalyzed in vitro by the calcium-dependent, leupeptin- and calpastatin-sensitive protease calpain-II purified from rat liver cytosol. Cleavage of the native 97-100 kDa reductase was enhanced by pretreatment (inactivation) of microsomes with ATP(Mg2+) and liver reductase kinase (compared to protein phosphatase-pretreated controls). This was reflected in a loss of the 97-100 kDa species and an increase in the soluble 52-56 kDa species (total enzyme activity and specific immunoblot recovery).
从大鼠肝脏胞质溶胶中纯化得到的钙依赖性、对亮抑酶肽和钙蛋白酶抑制蛋白敏感的钙蛋白酶II，在体外催化天然的97 - 100 kDa大鼠肝脏微粒体HMG CoA还原酶转化为膜结合的62 kDa和可溶性的52 - 56 kDa催化活性形式。与用蛋白磷酸酶预处理的对照相比，用ATP（Mg2+）和肝脏还原酶激酶对微粒体进行预处理（使其失活）可增强对天然97 - 100 kDa还原酶的切割。这表现为97 - 100 kDa条带的消失以及可溶性52 - 56 kDa条带的增加（总酶活性和特异性免疫印迹回收率）。
