ABSTRACT
In sarcoplasmic reticulum of rabbit skeletal muscles the activity of Ca2+, Mg2+- dependent ATPase was distinctly inhibited under effect of neuroleptic drugs - derivatives of phenothiazine and butyrophenone. The effect of tricyclic antidepressants was less pronounced. Tranquilizers (derivatives of 1,4-benzodiazepine) inhibited the enzyme, but trioxazin was only slightly active. High concentrations of lithium salts and of psychostimulants caffeine and corasole were found to stimulate the Ca2+, Mg2+-ATPase activity; low concentrations of the substances slightly inhibited the enzyme. The blocking effect of psychotropic drugs was more distinct, if the enzyme preparations were previously treated with ATP.
Subject(s)
Adenosine Triphosphatases/metabolism , Muscles/cytology , Psychotropic Drugs/pharmacology , Sarcoplasmic Reticulum/enzymology , Adenosine Triphosphatases/antagonists & inhibitors , Animals , Anti-Anxiety Agents/pharmacology , Antidepressive Agents, Tricyclic/pharmacology , Antipsychotic Agents/pharmacology , Benzodiazepines , Caffeine/pharmacology , Calcium/metabolism , Magnesium/metabolism , Pentylenetetrazole/pharmacology , Phenothiazines , RabbitsABSTRACT
The effect of neuroleptics, antidepressants, somnifacients and antiepileptic drugs on Na+- and K+-dependent transitions in the preparation of the transport ATP-ase from renal tubules of the guinea pig were looked into by using the spinal probes procedures. Neuroleptics inhibit most strongly (by 100--67 per cent) the conformant transition in the Na+- K+-dependent ATP-ase, their action manifesting itself to a greater extent with respect to the K+-dependent conformant transitions. The influence of antidepressants is close to that of the neuroleptics, although it is noticeably less intensive (78--46 per cent). The action of hypnotics (barbituric acid derivatives) and of antiepileptic drugs of a different chemical structure closely approaches, but is different from the effect of neuroleptics and antidepressants, both as concerns its intensity and the lack of any essential differences in the action upon the Na+- and K+-dependant conformant transitions.