Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Conformational changes of membrane-bound (Na+-K+)-ATPase as revealed by antibody inhibition


Koepsell,  Hermann
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Koepsell, H. (1979). Conformational changes of membrane-bound (Na+-K+)-ATPase as revealed by antibody inhibition. Journal of Membrane Biology, 45(1-2), 1-20. doi:10.1007/BF01869291.

Cite as: https://hdl.handle.net/21.11116/0000-0008-40B8-0
As different structural states of the (Na+−K+)-ATPase (EC may lead to a changed reactivity to antibodies, the influence of Na+, K+, Mg++, Pi and ATP on the reaction between highly purified (Na+−K+)-ATPase and antibodies directed against the membrane-bound enzyme was measured. The antigen antibody reaction was registered by measuring the antibody inhibition of (Na+−K+)-ATPase activity.

In themembrane-bound but not in thesolubilized enzyme four different degrees of antibody inhibition were obtained at equilibrium of the antigen antibody reaction if different combinations of Na+, K+, Mg++ and ATP were present during the incubation with the antibodies. Corresponding to the different degrees of inhibition, different rates of enzyme inhibition were measured. (a) The smallest degree of enzyme inhibition was obtained when (i) only Mg++, (ii) Mg++ and Na+ or (iii) Mg++ and K+ were present during the antigen antibody reaction. (b) The enzyme activity was inhibited more strongly if Na+, Mg++ and ATP were present together. (c) It was inhibited even more if only (i) Na+, (ii) K+, (iii) ATP or both (iv) ATP and Na+, (v) ATP and K+, (vi) ATP and Mg++, or if (vii) no ATP and activating ions were present. (d) The highest degree of antibody inhibition was obtained if Mg++, ATP and K+ were present together.

In the presence of Mg++ plus ADP and in the presence of Mg++ plus the ATP analog adenylyl (β-γ-methylene) diphosphonate, Nav and K+ did not influence the degree of antibody inhibition as they did in the presence of Mg++ plus ATP. It was further found that the degree of antibody inhibition in the presence of Mg++, ATP and K+ was affected by the sequence in which K+ and ATP were added to the enzyme prior to the addition of the antibodies.

It is suggested that by antibody inhibition different conformations of the (Na+−K+)-ATPase could be detected. These conformations may possibly not occur in the solubilized enzyme and therefore do not seem to be necessarily linked to the intermediary steps of the ATP hydrolysis of the enzyme. The structural changes which are induced by Na+ and K+ in the presence of Mg++ plus ATP are proposed to occur during the Na+−K+ transport.