Characterization of [ 35S] Lanthionine Ketimine Specific Binding to Bovine Brain Membranes

• Published in: Biochemical and biophysical research communications Vol. 195; no. 2; pp. 673 - 678
• Main Authors: Dupre, S., Fontana, M., Costa, M., Pecci, L., Ricci, G., Cavallini, D.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 15.09.1993; Elsevier
• Subjects: Adenylyl Cyclases - metabolism; Amino Acids, Sulfur - metabolism; Animals; Binding, Competitive; Biological and medical sciences; Brain - metabolism; Cattle; Cell Membrane - metabolism; Cell membranes. Ionic channels. Membrane pores; Cell structures and functions; Cerebral Cortex - metabolism; Erythrocyte Membrane - metabolism; Fundamental and applied biological sciences. Psychology; Kinetics; Molecular and cellular biology; Neurotransmitter Agents - pharmacology; Sulfur Radioisotopes; Turkeys; Vertebrata; Mammalia; Binding capacity; Bovine; Biomembrane; Artiodactyla; Catecholamine; Ungulata; Brain (vertebrata)
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1993.2098

[ 35S]Lanthionine ketimine binds specifically and with high affinity to bovine brain membranes (1). This binding has been studied in detail. It is reversible, not occurring at an uptake site or at a metabolizing enzyme and depending only weakly from ionic strength; it is affected by thiol reagents. [ 35S]Lanthionine ketimine specific binding is displaced only by other ketimines and by catecholamines, but not by more selective adrenergic ligands; binding parameters are reported. [ 3H]Adrenaline but not [ 3H]dihydroalprenolol is partially displaced by lanthionine ketimine. With bovine brain preparations a significant stimulation of basal adenylate cyclase activity by lanthionine ketimine is observed.