Persistence of species variation and regional heterogeneity of the apparent molecular masses of benzodiazepine-binding proteins after deglycosylation |
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Authors: | E Schmitz W Friedl R Reichelt J Hebebrand |
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Affiliation: | Institut für Humangenetik, Universit?t Bonn, FRG. |
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Abstract: | Brain membrane preparations of different vertebrates were photoaffinity labeled with [3H]flunitrazepam and subsequently deglycosylated with endoglycosidase F and peptide N-glycopeptidase. SDS-polyacrylamide gel electrophoresis followed by fluorography revealed that each benzodiazepine-binding protein is deglycosylated in two steps, indicating that each protein has two glycosylation sites. Species variation of the apparent molecular masses of the benzodiazepine-binding proteins and regional heterogeneity in avians persist after deglycosylation. These results indicate that the alpha-subunit(s) of the GABA/benzodiazepine receptor has undergone electrophoretically detectable changes in its amino acid composition during vertebrate evolution. The existence of at least two different alpha-subunits in avians is further substantiated. |
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