Comparison of two different benzodiazepine binding proteins by peptide mapping after limited proteolysis.
Proteins P51 and P55 were photolabeled by [3H]flunitrazepam, [3H]clonazepam or 3H-Ro 15-4513 and then compared by peptide mapping after limited digestion with various proteases. Results indicated that [3H]flunitrazepam or [3H]clonazepam irreversibly bind to the same and [3H]Ro 15-4513 to a different part of these proteins. The different radiolabeled peptide patterns obtained from P51 or P55, irrespective of the photolabel used, suggest a difference in the molecular structure of these proteins.
Sieghart
W
W
Department of Biochemical Psychiatry, Psychiatrische Universitätsklinik Wien, Vienna, Austria.
D000818:Animals; D001386:Azides / Q000378:metabolism; D001569:Benzodiazepines / Q000378:metabolism; D001665:Binding Sites; D001923:Brain Chemistry; D002531:Cerebellum / Q000032:analysis; D002998:Clonazepam / Q000378:metabolism; D005445:Flunitrazepam / Q000378:metabolism; D006624:Hippocampus / Q000032:analysis; D008970:Molecular Weight; D010449:Peptide Mapping; D051381:Rats; D011963:Receptors, GABA-A / Q000032:analysis* / Q000378:metabolism
D001386:Azides; D011963:Receptors, GABA-A; D001569:Benzodiazepines; D002998:Clonazepam; D005445:Flunitrazepam; C042957:Ro 15-4513