Ligand responses of alpha-bungarotoxin binding sites from skeletal muscle and optic lobe of the chick.
作者： S Molinaro , J Schmidt , G K Wang
DOI: 10.1016/S0021-9258(17)34320-X
关键词: Skeletal muscle 、 Nicotinic agonist 、 Biochemistry 、 Embryo 、 Biophysics 、 Ligand 、 Toxin 、 Binding site 、 Biology 、 Affinities 、 Receptor
摘要: Binding properties of detergent-solubilized receptors for alpha-bungarotoxin from skeletal muscle the 13th day chick embryo and optic lobe hatching were compared. It was found that both types receptor are nicotinic, although they differ in their affinities individual ligands rank order ligands. In contrast to receptor, neuronal binds toxin a reversible fashion (KD = 2.1 X 10(-10) M at 23 degrees C). Small inhibit brain equilibrium procedures. Toxin compete single type noninteracting site, ratio binding sites ligand-binding is unity. The inhibitory potency parallels ability, higher concentrations, accelerate . by interaction with same site on derived lobe.
sci-hub.st 参考文章(24)
A Maelicke, B W Fulpius, R P Klett, E Reich, Acetylcholine receptor. Responses to drug binding. Journal of Biological Chemistry. ,vol. 252, pp. 4811- 4830 ,(1977) , 10.1016/S0021-9258(17)40128-1
P M Salvaterra, H R Mahler, Nicotinic acetylcholine receptor from rat brain. Solubilization, partial purification, and characterization. Journal of Biological Chemistry. ,vol. 251, pp. 6327- 6334 ,(1976) , 10.1016/S0021-9258(20)81863-8
C. McQuarrie, P.M. Salvaterra, H.R. Mahlers, Studies on nicotinic acetylcholine receptors in mammalian brain. Interaction of solubilized protein with cholinergic ligands. Journal of Biological Chemistry. ,vol. 253, pp. 2743- 2747 ,(1978) , 10.1016/S0021-9258(17)40884-2
J. Patrick, B. Stallcup, alpha-Bungarotoxin binding and cholinergic receptor function on a rat sympathetic nerve line. Journal of Biological Chemistry. ,vol. 252, pp. 8629- 8633 ,(1977) , 10.1016/S0021-9258(19)75267-3
William M. Moore, Robert N. Brady, Studies of nicotinic acetylcholine receptor protein from rat brain: II. Partial purification Biochimica et Biophysica Acta. ,vol. 498, pp. 331- 340 ,(1977) , 10.1016/0304-4165(77)90271-9
Michel Weber, Jean-Pierre Changeux, Binding of Naja nigricollis (3H)alpha-toxin to membrane fragments from Electrophorus and Torpedo electric organs. II. Effect of cholinergic agonists and antagonists on the binding of the tritiated alpha-neurotoxin. Molecular Pharmacology. ,vol. 10, pp. 15- 34 ,(1974)
J. Schmidt, M.A. Raftery, A simple assay for the study of solubilized acetylcholine receptors Analytical Biochemistry. ,vol. 52, pp. 349- 354 ,(1973) , 10.1016/0003-2697(73)90036-5
A.W. Duggan, J.G. Hall, C.Y. Lee, Alpha-bungarotoxin, cobra neurotoxin and excitation of Renshaw cells by acetylcholine Brain Research. ,vol. 107, pp. 166- 170 ,(1976) , 10.1016/0006-8993(76)90106-2
Lloyd A. Greene, Binding of α-bungarotoxin to chick sympathetic ganglia: properties of the receptor and its rate of appearance during development Brain Research. ,vol. 111, pp. 135- 145 ,(1976) , 10.1016/0006-8993(76)91054-4
B.J. Morley, J.F. Lorden, G.B. Brown, G.E. Kemp, R.J. Bradley, Regional distribution of nicotinic acetylcholine receptor in rat brain. Brain Research. ,vol. 134, pp. 161- 166 ,(1977) , 10.1016/0006-8993(77)90935-0