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Isolation and N‐terminal amino acid sequence of an octopamine ligand binding protein
Author(s) -
Nathanson James A.,
Kantham Lakshmi,
Hunnicutt Edward J.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81508-x
Subject(s) - octopamine (neurotransmitter) , cyclase , biochemistry , photoaffinity labeling , phentolamine , receptor , peptide sequence , adenylate kinase , chemistry , biology , serotonin , gene
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.