Year: 1988
Type: article
Abstract: The glycoprotein nature of the ligand binding subunit of photoaffinity-labeled striatal D2 receptors was investigated. Upon photolysis, [125I]N-azidophenethylspiperone covalently incorporated into a major band of Mr 94000 with an appropriate pharmacological profile for D2 receptors as assessed by autoradiography following SDS-polyacrylamide gel electrophoresis. The exoglycosidase, neuraminidase, altered the electrophoretic mobility of the 94 kDa labeled band to 54 kDa with a slight modification in the binding affinity of [3H]spiperone. Endoglycosidase treatment (glycopeptidase-F) produced a further increase in the mobility of the 94 kDa peptide to approximately 43 kDa. A smaller specifically photolabeled D2 receptor peptide of 34 kDa does not contain terminal sialic acid but is an N-linked glycoprotein as assessed by lectin affinity chromatography and susceptibility to digestion by glycopeptidase-F to a peptide of approximately 23 kDa.
Source: FEBS Letters
Institution: University of Toronto
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Funder: Medical Research Council
OpenAlex ID: W1994263418