INHIBITION OF MEMBRANE-BOUND ADENOSINE TRIPHOSPHATASE WITH PLATINUM AND PALLADIUM SALTS

  • 1 January 1977
    • journal article
    • research article
    • Vol. 22  (3) , 418-423
Abstract
The inhibition capacity of Pt and Pd complexes [carcino-static substances] on membrane-bound [rabbit muscle] ATPase was studied. The degree of inhibition of the enzyme activity was determined by the nature of the central atom and by the electron density on it, and by the ligand donor-acceptor capacity and its mobility. The configuration of the complex and the charge of the complex ion were of importance. The acidoligands studied according to their inhibition effect on both Pt and Pd compounds were: NO2, Cl, Br, SCN and I. Pt and Pd complexes have different mechanisms of interaction with the enzyme.