The changes in conformation of (Na+ K+)-ATPase from rat brain membranes are accompanied by changes of protein segment movements in the nanosecond range
Language English Country Czech Republic Media print
Document type Journal Article
PubMed
2850590
Knihovny.cz E-resources
- MeSH
- Cell Membrane enzymology MeSH
- Fluorescein-5-isothiocyanate MeSH
- Fluoresceins MeSH
- Fluorescent Dyes MeSH
- Spectrometry, Fluorescence MeSH
- Rats, Inbred Strains MeSH
- Kinetics MeSH
- Protein Conformation MeSH
- Rats MeSH
- Brain metabolism MeSH
- Cerebral Cortex enzymology MeSH
- Sodium-Potassium-Exchanging ATPase metabolism MeSH
- Thiocyanates MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Fluorescein-5-isothiocyanate MeSH
- Fluoresceins MeSH
- Fluorescent Dyes MeSH
- Sodium-Potassium-Exchanging ATPase MeSH
- Thiocyanates MeSH
Differential polarized phase fluorometry of fluorescein-5-isothiocyanate (FITC) showed that the activation of (Na,K)-ATPase in crude plasma membranes from rat brain by 10 mmol.l-1 K+ and 100 mmol.l-1 Na+ significantly increased the rotational relaxational rate (R) of enzyme-bound FITC. This increase was blocked by both ouabain (0.1 mmol.l-1) and vanadate (0.1 mmol.l-1). In the absence of ATP, R was increased less after adding of 10 mmol.l-1 K+ to the membranes. The shifts in the nanosecond movements of the protein segments measured as R during the activation of (Na,K)-ATPase suggest that this type of movement might be of some functional importance.
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