Biochemical characterization of [3H]tryptamine binding sites from rat brain.
Rat brain membranes were treated with different protein modifying reagents, all of which were able to reduce [3H]tryptamine binding. However, inactivation by N-ethylmaleimide and iodoacetamide only was counteracted by coincubation with tryptamine. Thus, the [3H]tryptamine binding molecule is a membrane protein with an essential sulfhydryl group at the binding site. After incubation of digitonin-solubilized membranes with seven different lectins, no precipitation of [3H]tryptamine binding sites was observed. On concanavalin A and wheat germ agglutinin affinity chromatography, no [3H]tryptamine binding activity was found to be specifically bound. Therefore, the [3H]tryptamine binding protein appears to be devoid of lectin binding carbohydrate residues.
Brüning
G
G
Department of Anatomy, Free University, Berlin, F.R. Germany.
Rommelspacher
H
H
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002846:Chromatography, Affinity; D005033:Ethylmaleimide / Q000494:pharmacology; D005445:Flunitrazepam / Q000378:metabolism; D007700:Kinetics; D037102:Lectins; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D011957:Receptors, Opioid / Q000378:metabolism; D011985:Receptors, Serotonin / Q000302:isolation & purification / Q000378:metabolism*; D014363:Tryptamines / Q000378:metabolism*
D037102:Lectins; D011957:Receptors, Opioid; D011985:Receptors, Serotonin; D014363:Tryptamines; C030820:tryptamine; D005445:Flunitrazepam; D005033:Ethylmaleimide