Isolation and N-terminal amino acid sequence of an octopamine ligand binding protein.
An octopamine receptor photoaffinity probe was used to label membranes from the light organs of Photinus pyralis, a tissue highly enriched in octopamine receptors. Labeling was concentrated in a glycoprotein of 75 +/- 2 kDa with lesser labeling of a 79 +/- 2 kDa component. Labeling could be displaced by prior incubation with octopamine, mianserin, cyproheptadine, phentolamine or propranolol, with a relative potency that correlated with the ability of these same agents to modulate light organ octopamine-sensitive adenylate cyclase. The 75 kDa binding protein was isolated and its N-terminal amino acid sequence was determined.
Nathanson
J A
JA
Dept. of Neurology, Harvard Medical School, Massachusetts General Hospital, Boston 02114.
Kantham
L
L
Hunnicutt
E J
EJ
D000345:Affinity Labels; D000595:Amino Acid Sequence; D000818:Animals; D001386:Azides / Q000378:metabolism; D001517:Coleoptera; D007093:Imidazoles / Q000378:metabolism; D048289:Imidazolidines; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009655:Octopamine / Q000378:metabolism*; D011941:Receptors, Adrenergic / Q000302:isolation & purification* / Q000378:metabolism; D017982:Receptors, Biogenic Amine
D000345:Affinity Labels; D001386:Azides; D007093:Imidazoles; D048289:Imidazolidines; D011941:Receptors, Adrenergic; D017982:Receptors, Biogenic Amine; C027604:norsynephrine receptor; C060351:NC 5Z; D009655:Octopamine