Inhibition of sarcoplasmic reticulum Ca2+-ATPase by 2-mercaptoethanol.
The Ca2+-dependent ATPase activity of sarcoplasmic reticulum was inhibited when membrane vesicles were incubated at 0 degree C in presence of thiols. 2-mercaptoethanol was the most effective inhibitor from the thiols tested. The effect of 2-mercaptoethanol on the ATPase activity was biphasic; enzyme inhibition originally increased and then decreased with increasing thiol concentration. The inhibitory action of this thiol was significantly higher at low membrane concentrations and the rate of inactivation at 22 degrees C was considerably lower than that at 0 degree C. Ca2+-ATPase previously inhibited by 2-mercaptoethanol was partially reactivated by incubation with periodate.
Georgoussi
Z
Z
Sotiroudis
T G
TG
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D004793:Enzyme Reactivators; D066298:In Vitro Techniques; D008623:Mercaptoethanol / Q000494:pharmacology*; D010504:Periodic Acid / Q000494:pharmacology; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D004793:Enzyme Reactivators; D013438:Sulfhydryl Compounds; D010504:Periodic Acid; D008623:Mercaptoethanol; C009288:metaperiodate; D000252:Calcium-Transporting ATPases