Mar 1, 1976

Membrane-reversible H+-ATPase from Micrococcus lysodeikticus

European Journal of Biochemistry
E I MileykovskayaI A Kozlov


Treatment of phosphorylating fragments of bacterial membrane from Micrococcus lysodeikticus with trypsin leads to increase ATPase activity. As a result of this treatment, the membrane fragments acquire the ability to transform the ATP energy into transmembrane difference in potential. Dithiothreitol has a similar effect to that of trypsin on the membrane fragments from M. lysodeikticus. Dicyclohexylcarbodimide inhibits ATPase of the membrane fragments of M. lysodeikticus, and also the ATPase-reaction-coupled generation of membrane potential. It has been suggested that the increased ATPase activity of membranes from M. lysodeikticus during treatment with trypsin and dithiothreitol is connected with the effect of these agents on the protein inhibitor of ATPase.

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Mentioned in this Paper

Micrococcus luteus
Tissue Membrane
Adenosine Triphosphatases
Resting Potentials
Integral to Membrane
Oxidative Phosphorylation
DNA-dependent ATPase

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