Binding studies of polypeptide hormones to bovine neurophysins

J. A. Glasel, J. F. McKelvy, V. J. Hruby, A. F. Spatola

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

Experimental binding isotherms of [9 glycinamide 1 14C]oxytocin and [9 glycinamide 1 14C]arginine vasopressin to purified neurophysins I and II at pH = 4.4, 5.4, 6.5, 7.4, and 8.5 and 6°, 22°, and 37° in aqueous buffers are reported. For purposes of comparison, binding isotherms for [4 glycine 1 14C]oxytocin to neurophysin II and I in aqueous buffer, and [9 glycinamide 1 14C]oxytocin to neurophysin II in dimethylsulfoxide under selected conditions are also reported. A brief discussion of the interpretation of binding isotherms is entered into and apparent binding constants are derived. The results indicate that the interpretations presented in the literature up to now are much too simple. There are, in contrast, multiple binding sites of oxytocin and vasopressin to the neurophysins and large temperature dependences of the number of sites and their binding constants. We find, in fact, that at 37° the binding of neurohypophysial hormones to the supposed storage proteins is rather weak even at the pH of maximum binding.

Original languageEnglish (US)
Pages (from-to)2929-2937
Number of pages9
JournalJournal of Biological Chemistry
Volume251
Issue number10
StatePublished - Dec 1 1976

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Glasel, J. A., McKelvy, J. F., Hruby, V. J., & Spatola, A. F. (1976). Binding studies of polypeptide hormones to bovine neurophysins. Journal of Biological Chemistry, 251(10), 2929-2937.