[Applicability of the integral form of the Michaelis-Menten equation for the kinetic study of transport ATPases].
Applicability of the integrated form of the Michaelis-Menten equation to kinetic analysis of transport ATPases has been shown during continuous pH-metric recording of their activity. Two values of Km for both Na, K-ATPase and Ca-ATPase have been found to be consistent with the reported data. Both values of Km for Na, K-ATPase change with temperature, i. e. at 37 degrees, 26 degrees and 15 degrees C they are as follows: Km1--21, Km2--171; Km1--3.32, Km2--47; and Km1--1,2, Km2--20 microM, respectively. This method of determination of Km and V for transport ATPases compares favourably with the previously used methods in resulting efficiency.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001692:Biological Transport; D001921:Brain / Q000201:enzymology; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002417:Cattle; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D008433:Mathematics; D009132:Muscles / Q000201:enzymology; D011817:Rabbits; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism
D000251:Adenosine Triphosphatases; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase
Primenimost' integral'noĭ formy uravneniia Mikhaélisa-Menten dlia kineticheskogo issledovaniia transportnykh ATF-az.