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 |
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Hauptverfasser: | , , |
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 |
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ISSN: | 0007-4888 |
DOI: | 10.1007/s1017-01-77-0 |