Mutoh Y, Sugino A, Higashi K, Takasugi M, Kuroiwa A, Kawamura M
Division of Biology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan.
J UOEH. 1992 Dec 1;14(4):253-60. doi: 10.7888/juoeh.14.253.
The sarcoplasmic Ca(2+)-ATPase was reduced with 300 mM 2-mercaptoethanol at elevated temperatures (40-45 degrees C) with a concomitant loss of ATPase activity. The reduction and inactivation of the Ca(2+)-ATPase proceeded rapidly in the absence of Ca2+. The Ca(2+)-ATPase was also inactivated with 2-mercaptoethanol in the presence of diluted SDS (0.4 mg/ml) even at 20 degrees C. In contrast to the (Na+, K+) ATPase, the inactivated Ca(2+)-ATPase in the presence of diluted SDS was sedimented by the centrifugation at 100,000 x g for 30 min.
在高温（40 - 45摄氏度）下，肌浆网Ca(2 +)-ATP酶在300 mM 2 - 巯基乙醇作用下减少，同时ATP酶活性丧失。在没有Ca2 +的情况下，Ca(2 +)-ATP酶的减少和失活迅速发生。即使在20摄氏度，在稀释的SDS（0.4 mg/ml）存在下，Ca(2 +)-ATP酶也会被2 - 巯基乙醇失活。与(Na +, K +)ATP酶不同，在稀释的SDS存在下失活的Ca(2 +)-ATP酶在100,000 x g离心30分钟后会沉淀下来。
