Studies on the inhibition by propranolol of some human erythrocyte membrane enzymes and plasma cholinesterase.
Human erythrocyte acetylcholinesterase and the plasma cholinesterase variants are not only inhibited by propranolol but have been found to show stereospecificity for its isomers. The erythrocyte enzyme has a greater affinity for the L-isomer than either the racemate or the D-isomer. In contrast the plasma cholinesterases have greater specificity for the D-isomer than the other isomer or racemate. The usual enzyme shows greater stereospecificity than the atypical enzyme and these findings present additional evidence that these enzyme variants differ in structure at the catalytic active site. Neither Na+ + K+ -ATPase nor Mg2+-ATPase show stereo-specificity for the isomers of propranolol although both enzymes are inhibited by the drug. The action of the drug on the four enzymes in blood samples obtained from patients having Huntington's disease was found to be identical to those observed on the enzymes in blood samples from healthy controls.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors; D001665:Binding Sites; D017301:Ca(2+) Mg(2+)-ATPase; D002800:Cholinesterase Inhibitors; D002802:Cholinesterases / Q000097:blood*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D006816:Huntington Disease / Q000201:enzymology; D007527:Isoenzymes / Q000097:blood*; D007536:Isomerism; D011433:Propranolol / Q000494:pharmacology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors; D013379:Substrate Specificity
D002800:Cholinesterase Inhibitors; D007527:Isoenzymes; D011433:Propranolol; D002802:Cholinesterases; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D000254:Sodium-Potassium-Exchanging ATPase