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- W1994263418 abstract "The glycoprotein nature of the ligand binding subunit of photoaffinity‐labeled striatal D 2 receptors was investigated. Upon photolysis, [ 125 I] N ‐azidophenethylspiperone covalently incorporated into a major band of M r , 94000 with an appropriate pharmacological profile for D 2 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 [ 3 H]spiperone. Endoglycosidase treatment (glycopeptidase‐F) produced a further increase in the mobility of the 94 kDa peptide to ∼43 kDa. A smaller specifically photolabeled D 2 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 ∼23 kDa." @default.
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- W1994263418 date "1988-01-25" @default.
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- W1994263418 title "Glycoprotein nature of D<sub>2</sub>dopamine receptors" @default.
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- W1994263418 doi "https://doi.org/10.1016/0014-5793(88)80902-5" @default.
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