[Kinetic properties of the Ca2+--ATPase in the skeletal muscle sarcolemma of the rabbit normally and in E-avitaminotic dystrophy].
The article deals with values of seeming Michaelis' constants (for ATP) obtained at different temperatures and Michaelis' constants (for Ca ATP) obtained at 30degrees C with pathology and in norm for sarcolemma Ca2+-ATPase. It follows from the analysis of the Ca2+ total concentration effect (the ATP total concentration being constant) on the activation energy of ATP hydrolysis reactions that with pathology sarcolemma possesses, evidently, a greater adsorption affinity to Ca2+ (the enzyme activator) than in norm. The thermoinactivation properties of the enzyme are studied. It is shown that the inactivation coefficient with pathology increases more rapidly with a temperature rise than in norm. It indicates to the fact that the enzyme from the dystrophic muscles is more labile to the heat effect than from the normal ones.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation; D004794:Enzyme Repression; D007700:Kinetics; D009137:Muscular Dystrophy, Animal / Q000201:enzymology*; D011817:Rabbits; D012508:Sarcolemma / Q000201:enzymology*; D013696:Temperature; D014811:Vitamin E Deficiency / Q000201:enzymology*
D000251:Adenosine Triphosphatases; D002118:Calcium
Kinetychni vlastyvosti Ca2+-ATFaszy sarkolemy skeletnykh krolia v normi ĭ za E-avitaminoznoĭ dystrofiĭ.