Abstract
Halide complexes of platinum have been previously shown to inhibit tumors and cell growth as well as to possess immunosuppresive activity. Evidence is presented here that the active species in Rb 2PtBr 4 solutions which inhibits both leucine aminopeptidase ( l-leucyl-peptide hydrolase, EC 3.4.1.1) and malate dehydrogenase ( l-malate:NAD + oxidoreductase, EC 1.1.1.37) enzymes is PtBr 3(H 2O) −. The aquo complex earlier has been shown to be in equilibrium with PtBr 4 2− in solution and the rate of formation is known. This is in accord with the rate of inhibition of enzyme activity by fresh solutions of Rb 2PtBr 4. This reagent should provide another method for studying the active site and function of enzymes.
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