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Peptide Subunits of γ‐Aminobutyric Acid A /Benzodiazepine Receptors from Bovine Cerebral Cortex
Author(s) -
Park Dongeun,
Blas Angel L.
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb03455.x
Subject(s) - photoaffinity labeling , flunitrazepam , chemistry , peptide , muscimol , gel electrophoresis , antiserum , biochemistry , polyacrylamide gel electrophoresis , receptor , gabaa receptor , biology , antibody , enzyme , immunology
The γ‐aminobutyric acid A /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 β subunit [57,000 M r band in sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE)] is composed of at least four different peptides of 54,000–57,000 M r . Two peptides of 55,000 and 57,000 M r were recognized by the β subunit‐specific monoclonal antibody 62‐3G1. Peptides in the range of 54,000–57,000 M r were photoaffinity‐labeled with [ 3 H]muscimol. A different 57,000 M r peptide was photoaffinity‐labeled by [ 3 H]flunitrazepam, but neither was recognized by the monoclonal antibody 62‐3G1 nor photoaffinity‐labeled with [ 3 H]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 M r were also photoaffinity‐labeled by [ 3 H]flunitrazepam and reacted with antiserum A. However, the 57,000 M r peptide that also was photoaffinity‐labeled by [ 3 H]flunitrazepam did not react with antiserum A.