Abstract

Inhibition of three glycolytic enzymes by NaF and Na₂PO₃F^? in isolated rat hepatocytes has been demonstrated. The data indicate that incubation of hepatocytes with NaF or MFP and subsequent removal of NaF and MFP results in a significant inhibition of enolase (E.C. 4.2.1.11), phosphoglucomutase (E.C. 2.7.5.1.), and pyruvate kinase (E.C. 2.7.1.40). It is suggested that the fluorine compound enters the hepatocyte, becomes bound to the enzyme (phosphoglucomutase and enolase) and inhibits its activity. The inhibition of pyruvate kinase may be due to a cAMP dependent phosphorylation of the enzyme.

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