Reduction and inactivation of the sarcoplasmic Ca(2+)-ATPase by 2-mercaptoethanol--contrast to the (Na+,K+) ATPase.
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.
Mutoh
Y
Y
Division of Biology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan.
Sugino
A
A
Higashi
K
K
Takasugi
M
M
Kuroiwa
A
A
Kawamura
M
M
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D008623:Mercaptoethanol / Q000494:pharmacology*; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013696:Temperature
D008623:Mercaptoethanol; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase