Isolation, characterization, and purification to homogeneity of an endogenous polypeptide with agonistic action on benzodiazepine receptors.

@article{Guidotti1983IsolationCA,
  title={Isolation, characterization, and purification to homogeneity of an endogenous polypeptide with agonistic action on benzodiazepine receptors.},
  author={Alessandro Guidotti and Concetta M. Forchetti and Maria Giuseppa Corda and D. Konkel and Carl D. Bennett and Erminio Costa},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1983},
  volume={80 11},
  pages={
          3531-5
        }
}
  • A. GuidottiC. Forchetti E. Costa
  • Published 1 June 1983
  • Biology, Chemistry
  • Proceedings of the National Academy of Sciences of the United States of America
A brain polypeptide termed diazepam-binding inhibitor (DBI) and thought to be chemically and functionally related to the endogenous effector of the benzodiazepine recognition site was purified to homogeneity. This peptide gives a single band of protein on NaDodSO4 and acidic urea gel electrophoresis. A single UV-absorbing peak was obtained by HPLC using three different columns and solvent systems. DBI has a molecular mass of approximately equal to 11,000 daltons. Carboxyl-terminus analysis… 

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