[Nonhyperbolic kinetics of Na,K-ATPase--a new viewpoint].
The kinetics of the 130 kDa monomer obtained by treatment of duck salt gland Na,K-ATPase with C12E8 was compared with that of the membrane-bound enzyme. The shapes of the substrate-velocity curves for the membrane-bound and solubilized forms were quite different: a hyperbolic one for the monomeric Na,K-ATPase and a nonhyperbolic one for the native enzyme. A reaction scheme for ATP hydrolysis based on a comparative analysis of kinetic properties of these two forms is proposed. Experimental evidence in favour of this hypothesis is presented.
Fedosova
N U
NU
Boldyrev
A A
AA
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D003902:Detergents; D004372:Ducks; D006868:Hydrolysis; D007700:Kinetics; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013379:Substrate Specificity
D003902:Detergents; D000254:Sodium-Potassium-Exchanging ATPase
Negiperbolicheskaia kinetika Na,K-ATPazy--novyĭ vzgliad na problemy.