Principles of selectivity of sodium and potassium binding sites of the Na+/K+-ATPase. A corollary hypothesis
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články
PubMed
2849999
DOI
10.1016/0005-2736(88)90465-8
PII: 0005-2736(88)90465-8
Knihovny.cz E-zdroje
- MeSH
- chemické modely MeSH
- draslík metabolismus MeSH
- krysa rodu Rattus MeSH
- matematika MeSH
- myokard enzymologie MeSH
- sarkolema enzymologie MeSH
- sodík metabolismus MeSH
- sodíko-draslíková ATPasa metabolismus MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- draslík MeSH
- sodík MeSH
- sodíko-draslíková ATPasa MeSH
The mechanisms whereby the sodium and potassium binding sites of heart sacrolemmal Na+/K+-ATPase (EC 3.6.1.3) distinguished between monovalent cations were investigated using methods of enzyme kinetics. The properties of the sodium binding sites were studied in the presence of 2,4,6-trinitrobenzenesulfonic acid in concentrations completely inhibiting the action of potassium on the enzyme. To test the selectivity of potassium binding sites, K+-p-nitrophenylphosphatase activity was employed as a model. The results suggest that the selectivity of Na+- and K+-binding sites of Na+/K+-ATPase may be due to two independent mechanisms: (i) The principle of key and lock (formation of coordination bounds); (ii) Optimal difference between solvatation energy (in the specific binding site) and hydration enthalpy of the respective cation.
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