The binding of [3H] pargyline to rat liver mitochondrial monoamine oxidase.
The synthesis and purification of tritium labelled N-desmethylpargyline and pargyline are described. The suitability of these irreversible suicide inhibitors of monoamine oxidase (MAO) as ligands in binding studies to rat liver mitochondrial MAO has been evaluated. [3H] Pargyline was found to be more satisfactory than its N-desmethyl analogue because of its greater potency and lower proportion of non-specific binding. The binding of pargyline reached saturation when about 31 pmol mg protein-1 was bound. It was not possible to explain the time course of the binding by either simple first or second-order kinetics. [3H]-Pargyline is a potentially valuable ligand for the estimation of the concentration of NAO active centres without the need to remove the enzyme from the mitochondrial membrane.
D000818:Animals; D001667:Binding, Competitive; D066298:In Vitro Techniques; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology*; D008995:Monoamine Oxidase / Q000378:metabolism*; D008996:Monoamine Oxidase Inhibitors; D010293:Pargyline / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D051381:Rats; D013997:Time Factors; D014191:Tranylcypromine / Q000494:pharmacology
D008996:Monoamine Oxidase Inhibitors; D014191:Tranylcypromine; D010293:Pargyline; D008995:Monoamine Oxidase