Limited Tryptic Proteolysis of the Benzodiazepine Binding Proteins in Different Species Reveals Structural Homologies |
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Authors: | Waltraut Friedl Klaus-Ulrich Lentes Elke Schmitz Peter Propping Johannes Hebebrand |
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Affiliation: | Institut für Humangenetik, Universit?t Bonn, F.R.G. |
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Abstract: | Peptide mapping can be used to elucidate further the structural similarities of the benzodiazepine binding proteins in different vertebrate species. Crude synaptic membrane preparations were photoaffinity-labeled with [3H]flunitrazepam and subsequently degraded with various concentrations of trypsin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by fluorography allowed a comparison of the molecular weights of photolabeled peptides in different species. Tryptic degradation led to a common peptide of 40K in all species investigated, a finding indicating that the benzodiazepine binding proteins are structurally homologous in higher bony fishes and tetrapods. |
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Keywords: | Benzodiazepine receptors Species variation Tryptic degradation Gene duplication Photoaffinity labeling |
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