E31-K352, the Minimal Cation Binding Moiety of Na+,K+-ATPase
Copyright policy )E31-K352, the Minimal Cation Binding Moiety of Na+,K+-ATPase
Upon limited tryptic fragmentation of Na+,K(+)-ATPase a 35 kDa fragment (E31-K352) was formed that bound 204Tl+ on blot. Further fragmentation led to loss of binding, pointing to the conclusion that E31-K352 is the minimal cation binding unit in Na+,K(+)-ATPase.
- Radboud University Nijmegen Netherlands
Membrane Proteins, Mechanisme en functie van oscillerende second messenger systemen, Kidney, Peptide Fragments, Mechanism and function of oscillating second messenger systems, Molecular Weight, Cations, Animals, Electrophoresis, Polyacrylamide Gel, Trypsin, Rabbits, Sodium-Potassium-Exchanging ATPase, Tellurium, Protein Binding
Membrane Proteins, Mechanisme en functie van oscillerende second messenger systemen, Kidney, Peptide Fragments, Mechanism and function of oscillating second messenger systems, Molecular Weight, Cations, Animals, Electrophoresis, Polyacrylamide Gel, Trypsin, Rabbits, Sodium-Potassium-Exchanging ATPase, Tellurium, Protein Binding
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).4 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Average impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!