[35S]tert.-butylbicyclophosphorothionate and avermectin bind to different sites associated with the gamma- aminobutyric acid-benzodiazepine receptor complex.
Low concentrations of avermectin B1a (AVM) stimulated the specific high affinity binding of [35S]tert.-butylbicyclophosphorothionate [( 35S]TBPT) to membranes from rat cerebral cortex in the absence or presence of chloride or bromide ions. In contrast, TBPT either weakly stimulaes or does not significantly influence the specific high affinity binding of [3H]AVM to the same membranes in the absence or presence of chloride ions, respectively. These results indicate that [3H]AVM and [35S]TBPT bind to different but closely associated binding sites.
D000818:Animals; D001665:Binding Sites; D001643:Bridged Bicyclo Compounds / Q000378:metabolism*; D019086:Bridged Bicyclo Compounds, Heterocyclic; D001952:Bridged-Ring Compounds / Q000378:metabolism*; D002531:Cerebellum / Q000378:metabolism; D002540:Cerebral Cortex / Q000378:metabolism*; D006624:Hippocampus / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007559:Ivermectin / Q000031:analogs & derivatives*; D007783:Lactones / Q000378:metabolism*; D008566:Membranes / Q000378:metabolism; D051381:Rats; D011963:Receptors, GABA-A / Q000378:metabolism*
D001643:Bridged Bicyclo Compounds; D019086:Bridged Bicyclo Compounds, Heterocyclic; D001952:Bridged-Ring Compounds; D007783:Lactones; D011963:Receptors, GABA-A; D007559:Ivermectin; C037476:tert-butylbicyclophosphorothionate; C019264:avermectin