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Literature DB >> 1237294

Co-operative binding of oxytocin to bovine neurophysin II.

Abstract

The interaction of oxytocin with bovine neurophysin II in 0.1 M-sodium phosphate, pH 5.8, was investigated by equilibrium-dialysis and sedimentation studies. Sigmoidality of the binding curve is attributed to isomerization, either hormone-induced or pre-existing, with preferential binding of oxytocin to one isomeric state. Results are consistent with a binding equation of the form r = (2P[S]+2PQ[S]2)/(1+2P[S]+PQ[S]2) and values of 0.7 X 10(5)M-1 and 1.3 X 10(5)M-1 for P and Q respectively. The significance of these two parameters in relation to current theories of allostery is also discussed.

Entities: Chemical Gene Species

Mesh：

Substances：
Neurophysins
Oxytocin

Year: 1975 PMID： 1237294 PMCID： PMC1165455 DOI： 10.1042/bj1470377

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

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References

17 in total

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Authors: M D Hollenberg; D B Hope
Journal: Biochem J Date: 1968-01 Impact factor: 3.857

Co-operative binding of oxytocin to bovine neurophysin II.

1. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

2. [Oxytocin and vasopressin of sheep: reconstitution of an active hormonal complex].

3. Purification of oxytocin and vasopressin by way of a protein complex.

4. The interaction of ribonuclease with purine and pyrimidine phosphates. I. Binding of adenosine 5'-monophosphate to ribonuclease.

5. Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits.

6. Synthesis of oxytocin: suppression of dimer formation.

7. Physical and chemical properties of the bovine neurophysins.

8. The binding of oxytocin and oxytocin analogues by purified bovine neurophysins.

9. Comparison of experimental binding data and theoretical models in proteins containing subunits.

10. The isolation of the native hormone-binding proteins from bovine pituitary posterior lobes. Crystallization of neurophysin-I and-II as complexes with [8-arginine]-vasopressin.