Related Experiment Video
Updated: Aug 8, 2026

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
Published on: October 17, 2014
Comparison of the kinetic properties of membrane-bound and solubilized Na,K-ATPase
1Department of Biochemistry, Moscow State University, U.S.S.R.
Abstract:
Substrate-velocity curve for Na,K-ATPase under optimal conditions is described as a curve with intermediary plateau. C12E2 treatment of the enzyme changes its kinetic behaviour. The substrate-velocity curve transforms into hyperbolic one and the Km value for the solubilized enzyme approaches the Km value for the first phase of the complex curve. The experimental substrate-velocity curves obtained for Na,K-ATPase under different conditions were analyzed on the basis of the sum of Michaelis and Hill equations and the kinetic scheme for the enzyme was proposed. This model suggests that at the definite step of the reaction cycle the short-living oligomer is formed which can bind ATP with higher affinity thus accelerating E2----E1 transition. Several additional experimental facts that prove the hypothesis are presented.
Related Concept Videos
Primary Active Transport
Primary Active Transport
ATP Driven Pumps I: An Overview
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
ATP Synthase: Mechanism
ATP Driven Pumps III: V-type Pumps
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Active Transport
Primary active transporters, like Na+, K+ and -ATPase, directly utilize ATP to move ions across the membrane. These transporters play significant roles in various physiological processes. For instance, Na+, K+ and -ATPase maintain...

