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 language | English (US) |
|---|---|
| Pages (from-to) | 2929-2937 |
| Number of pages | 9 |
| Journal | Journal of Biological Chemistry |
| Volume | 251 |
| Issue number | 10 |
| State | Published - 1976 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Binding studies of polypeptide hormones to bovine neurophysins. / Glasel, J. A.; McKelvy, J. F.; Hruby, Victor J; Spatola, A. F.
In: Journal of Biological Chemistry, Vol. 251, No. 10, 1976, p. 2929-2937.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding studies of polypeptide hormones to bovine neurophysins
AU - Glasel, J. A.
AU - McKelvy, J. F.
AU - Hruby, Victor J
AU - Spatola, A. F.
PY - 1976
Y1 - 1976
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0017063882&partnerID=8YFLogxK
M3 - Article
C2 - 5446
AN - SCOPUS:0017063882
VL - 251
SP - 2929
EP - 2937
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 10
ER -