[Inhibitory effect platinum and palladium complexes as indicator of conformational changes in sarcoplasmic reticulum membranes].
Inhibition of Ca2+-dependent ATPase of sarcoplasmic reticulum membranes (SRM) by platinum and palladium complexes is considerable enhanced during the incubation of these compunds with SRM preparations in the presence of small (10(-5) M) concentrations of ATP or ADP. AMP and nucleotides with non-adenine bases do not have inhibitory effect. To increase the sensitivity of Ca2+-dependent ATPase to platinum and palladium complexes under the action of ATP (but not ADP), the presence of free Ca2+-ions in the medium is required. In the absence of ATP Ca2+-ions do not affect the inhibiting effect of the complexes. The increase in pH of the medium up to 8.5 and the increase of temperature up to 45degree C sharply decrease the ATP ability to enchance the sensitivity of Ca2+-dependent  ATPase to platinum and palladium compunds. It is assumed that the ATP ability to enhance  Ca2+-dependent ATPase inhibition by platinum and palladium complexes is due to ATP-dependent structural changes in SRM, which increase the availability of certain groups of the enzyme to those compounds.
[Inhibitory effect platinum and palladium complexes as indicator of conformational changes in sarcoplasmic reticulum membranes]. Inhibition of Ca2+-dependent ATPase of sarcoplasmic reticulum membranes (SRM) by platinum and palladium complexes is considerable enhanced during the incubation of these compunds with SRM preparations in the presence of small (10(-5) M) concentrations of ATP or ADP. AMP and nucleotides with non-adenine bases do not have inhibitory effect. To increase the sensitivity of Ca2+-dependent ATPase to platinum and palladium complexes under the action of ATP (but not ADP), the presence of free Ca2+-ions in the medium is required. In the absence of ATP Ca2+-ions do not affect the inhibiting effect of the complexes. The increase in pH of the medium up to 8.5 and the increase of temperature up to 45degree C sharply decrease the ATP ability to enchance the sensitivity of Ca2+-dependent  ATPase to platinum and palladium compunds. It is assumed that the ATP ability to enhance  Ca2+-dependent ATPase inhibition by platinum and palladium complexes is due to ATP-dependent structural changes in SRM, which increase the availability of certain groups of the enzyme to those compounds.