MgATP-induced inhibition of the enzymic activity of chloroform-released ox-heart mitochondrial ATPase
Preincubation of the chloroform-released ox-heart mitochondrial ATPase with its substrate, MgATP, results in a time-dependent inhibition of its ATPase activity. The inhibition is irreversible on the time-scale of an ATPase assay. It is not due to the accumulation of ADP and P i. The extent of the in...
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Veröffentlicht in: | Biochemical and biophysical research communications 1979-11, Vol.91 (2), p.599-605 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Preincubation of the chloroform-released ox-heart mitochondrial ATPase with its substrate, MgATP, results in a time-dependent inhibition of its ATPase activity. The inhibition is irreversible on the time-scale of an ATPase assay. It is not due to the accumulation of ADP and P
i. The extent of the inhibition is proportional to the number of turnovers of the enzyme during the preincubation period. It is suggested that the MgATP-induced inhibition described here is due to an intermediate enzyme-substrate complex of the ATP-hydrolytic pathway becoming converted into an inhibited enzyme species. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(79)91564-X |