Two unexplained kinetic features of NA,K-ATPase may be understood as indicating K(+)-induced cooperativity between subunits in a dimeric enzyme.
Plesner
I W
IW
Department of Chemistry, University of Aarhus, Denmark. IWP@kemi.aau.dk
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D019281:Dimerization; D007700:Kinetics; D046911:Macromolecular Substances; D008956:Models, Chemical; D011188:Potassium / Q000378:metabolism* / Q000494:pharmacology; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*
D046911:Macromolecular Substances; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium