Bomebesin: specific binding to rat brain membranes.
The binding of a radiolabeled bomebesin analogue to rat brain membranes was studied. [125I-Tyr4]Bombesin bound with high affinity (KD = 3 nM) to a single class of non-interacting sites. Binding was specific, saturable (3.8 pmol of sites/g of wet tissue), and reversible. Regional and subcellular distribution studies showed that the density of sites was 7-fold greater in the hippocampus than the medulla/pons and greater in synaptosomal fractions than in mitochondrial or nuclear fractions. The abilities of numerous bombesin analogues to induce hypothermia and to inhibit [125I-Tyr4]bombesin-binding activity correlate well. Numerous amino acid residues near the CONH2-terminal are required for high-affinity binding and biological potency.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D001839:Bombesin / Q000378:metabolism*; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D007700:Kinetics; D008297:Male; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D013329:Structure-Activity Relationship
D010455:Peptides; D001839:Bombesin