[Inhibition of membrane-bound adenosine triphosphatase by platinum and palladium salts].
Inhibition capacity of platinum and palladium complexes is studied on membrane-bound ADTP. The degree of inhibition of the enzyme activity is determined by the nature of the central atom and by the electron density on it, as well as by the ligand donor-acceptor capacity, by its mobility. The configuration of the complex and the charge of complex ion are of importance. The acidoligands studied according to their inhibition effect can be arranged in the following line: NO2, Cl, Br, SCN, I, which is true both for platinum and palladium compounds. For palladium complexes this line coincides with the location of ligands according to their ability to draw off the electron density from the central atom while in case of platinum complexes it has an opposite course of relationship for platinum and palladium complexes, points to a different mechanism of their interaction with the enzyme.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D002118:Calcium / Q000378:metabolism; D008274:Magnesium / Q000494:pharmacology; D008968:Molecular Conformation; D010165:Palladium / Q000494:pharmacology*; D010984:Platinum / Q000494:pharmacology*; D012492:Salts / Q000494:pharmacology; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013329:Structure-Activity Relationship
D012492:Salts; D010984:Platinum; D010165:Palladium; D000251:Adenosine Triphosphatases; D008274:Magnesium; D002118:Calcium
Ingibirovanie membranosviazannoĭ adenozintrifosfatazy soliami platiny i palladiia.