Substrate specificity of [Na.sup.+],[Cl.sup.-]-ATpase

We studied substrate specificity of [Na.sup.+],[Cl.sup.-](HC[O.sup.-.sub.3]))-ATPase. In most cases, replacement of ATP for other phosphate-containing substances resulted in not only pronounced suppression of phosphohydrolase reactions, but also dramatic changes of their responsiveness to the stimul...

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Veröffentlicht in:Bulletin of experimental biology and medicine 2016-09, Vol.161 (5), p.651
Hauptverfasser: Yurkiv, V.A, Melikhov, V.I, Shubin, V.S
Format: Artikel
Sprache:eng
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Zusammenfassung:We studied substrate specificity of [Na.sup.+],[Cl.sup.-](HC[O.sup.-.sub.3]))-ATPase. In most cases, replacement of ATP for other phosphate-containing substances resulted in not only pronounced suppression of phosphohydrolase reactions, but also dramatic changes of their responsiveness to the stimulating effect of monovalent ions. The data showed that [Na.sup.+],[Cl.sup.-](HC[O.sup.-.sub.3])-ATPase is a highly specific enzyme for ATP. Key Words: secretory process; small intestine; [Na.sup.+],[Cl.sup.-](HC[O.sup.-.sub.3])-ATPase; CFTR protein
ISSN:0007-4888
DOI:10.1007/s1017-01-77-0