PMID: 239193Mar 1, 1975Paper

Drug-biomolecule interactions: proton magnetic resonance studies of complex formation between bovine neurophysins and oxytocin at molecular level

Journal of Pharmaceutical Sciences
J H GriffinM Camier

Abstract

Proton magnetic resonance spectroscopy was used to monitor individual amino acid residues in bovine neurophysin, in the nonapeptide hormone oxytocin, and in the complex formed between them. For neurophysin I alone, a normal titration curve for the C-2 proton resonance of the lone histidine residue was obtained with an apparent ionization constant of 6.9 addition of oxytocin to a solution of neurophysin I at pH 6.5 resulted in several changes in the spectrum. The effect on the histidine C-2 proton resonance signal indicated a slow exchange process between two states, probably representing a conformational change in the protein. The apparent pK of the histidine residue in the hormonal complex was shifted to 6.7, indicating a slightly more positive (less electron dense) environment for the histidine residue. Resonances of the single tyrosine residue of oxytocin were observed to broaden significantly, but not to shift appreciably, on the addition of neurophysin II. These observations may indicate involvement of the tyrosyl residue of oxytocin in the hormone-"carrier protein" interaction.

References

Sep 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·H F EpsteinJ S. Cohen
May 31, 1972·Journal of the American Chemical Society·R NoyoriH Takaya
Jul 16, 1971·Biochemical and Biophysical Research Communications·R WalterJ D Capra
Aug 1, 1966·Proceedings of the National Academy of Sciences of the United States of America·E Breslow, L Abrash
Jul 1, 1968·Proceedings of the National Academy of Sciences of the United States of America·D H MeadowsH A Scheraga
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Jan 8, 1971·Biochemical and Biophysical Research Communications·S Ogawa, R G Shulman

Citations

Sep 1, 1994·International Journal of Peptide and Protein Research·H HuangE Breslow
Feb 1, 1983·International Journal of Peptide and Protein Research·V Virmani-Sardana, E Breslow

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