Article date: 1991/6/1
PubMed ID: 1851209
Journal name: Journal of neurochemistry (ISSN: 0022-3042)
The gamma-aminobutyric acidA/benzodiazepine receptor complexes from bovine cerebral cortex were purified by immunoaffinity chromatography, and the main component peptide subunits were characterized. The peptide band originally thought to be a single beta subunit [57,000 Mr band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)] is composed of at least four different peptides of 54,000-57,000 Mr. Two peptides of 55,000 and 57,000 Mr were recognized by the beta subunit-specific monoclonal antibody 62-3G1. Peptides in the range of 54,000-57,000 Mr were photoaffinity-labeled with [3H]muscimol. A different 57,000 Mr peptide was photoaffinity-labeled by [3H]flunitrazepam, but neither was recognized by the monoclonal antibody 62-3G1 nor photoaffinity-labeled with [3H]muscimol. Some peptides could be identified by their differential mobility shift in SDS-PAGE after treatment with endoglycosidase H. Two additional subunit peptides of 51,000 and 53,000 Mr were also photoaffinity-labeled by [3H]flunitrazepam and reacted with antiserum A. However, the 57,000 Mr peptide that also was photoaffinity-labeled by [3H]flunitrazepam did not react with antiserum A.
Author List: Park D, de Blas A L
Publication Types: Journal Article; Research Support, U.S. Gov't, P.H.S.
Substances mentioned in the article: Affinity Labels; Neuropeptides; Peptide Fragments; Receptors, GABA-A; Muscimol; Flunitrazepam;
Mesh terms: Affinity Labels; Animals; Cattle; Cerebral Cortex/metabolism; Flunitrazepam/metabolism; Glycosylation; Muscimol/metabolism; Neuropeptides/metabolism; Peptide Fragments/metabolism; Peptide Mapping; Precipitin Tests; Receptors, GABA-A/metabolism;