Isolation of a third bovine neurophysin

Biochem J. 1969 Nov;115(3):473-9. doi: 10.1042/bj1150473.

Abstract

1. A third native hormone-binding protein, neurophysin-C, has been isolated from acetone-desiccated bovine pituitary posterior lobes. 2. This protein was detected in lysates of neurosecretory granules isolated from bovine pituitary posterior lobes. 3. The molecular weight appears to be close to 10000. 4. Neurophysin-C is similar in amino acid composition to neurophysin-I and -II; it contains a single residue of tyrosine and of methionine. The N-terminal amino acid in all three neurophysins is alanine. 5. Neurophysin-C accounts for approximately 15% of the total hormone-binding protein present in the pituitary posterior lobes. 6. The new neurophysin forms complexes with oxytocin as well as with [8-arginine]-vasopressin. The complex with vasopressin has been crystallized. 7. Bioassay of the pressor and oxytocic activities of the protein-hormone complexes shows that neurophysin-C binds one molecule of either vasopressin or oxytocin.

MeSH terms

  • Acetone
  • Alanine / analysis
  • Amino Acids / analysis
  • Animals
  • Biological Assay
  • Cattle
  • Methionine / analysis
  • Molecular Weight
  • Oxytocin
  • Pituitary Gland, Posterior / analysis
  • Pituitary Hormones, Posterior / isolation & purification*
  • Protein Binding
  • Tyrosine / analysis
  • Vasopressins

Substances

  • Amino Acids
  • Pituitary Hormones, Posterior
  • Vasopressins
  • Acetone
  • Tyrosine
  • Oxytocin
  • Methionine
  • Alanine