The changes in conformation of (Na+ K+)-ATPase from rat brain membranes are accompanied by changes of protein segment movements in the nanosecond range
Jazyk angličtina Země Česko Médium print
Typ dokumentu časopisecké články
PubMed
2850590
Knihovny.cz E-zdroje
- MeSH
- buněčná membrána enzymologie MeSH
- fluorescein-5-isothiokyanát MeSH
- fluoresceiny MeSH
- fluorescenční barviva MeSH
- fluorescenční spektrometrie MeSH
- inbrední kmeny potkanů MeSH
- kinetika MeSH
- konformace proteinů MeSH
- krysa rodu Rattus MeSH
- mozek metabolismus MeSH
- mozková kůra enzymologie MeSH
- sodíko-draslíková ATPasa metabolismus MeSH
- thiokyanatany MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- fluorescein-5-isothiokyanát MeSH
- fluoresceiny MeSH
- fluorescenční barviva MeSH
- sodíko-draslíková ATPasa MeSH
- thiokyanatany 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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