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pubmed:abstractText |
Investigations have been made of the kinetic effects of the antibiotic aurovertin on the ATPase and ITPase activity of isolated rat liver mitochondrial ATPase. Unusual patterns of inhibition, decreasing slope, and increasing y-intercept values of double reciprocal plots, were observed with Mg-ATP as the substrate under various conditions. Under specified conditions, aurovertin stimulated hydrolysis of MgATP. The inhibition of MgITP hydrolysis was uncompetitive. Aurovertin eliminated the HCO3-minus stimulation of MgATP hydrolysis. The implications of these findings for the mechanism of mitochondrial ATPase are briefly discussed.
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