Complete amino acid sequence of a VLDV-type neurophysin from ostrich differs markedly from known mammalian neurophysins
| Autor: | Ryno J. Naudé, Claude Lazure, Hesta S. Saayman, Michel Chrétien, Willem Oelofsen |
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| Rok vydání: | 1987 |
| Předmět: |
Mammals
Neurophysins Vasopressin Chemistry Binding protein Neurohypophyseal Hormones Molecular Sequence Data Oxytocin Biochemistry Arginine Vasopressin Birds medicine.anatomical_structure Pituitary Gland Posterior Posterior pituitary medicine Animals Amino Acid Sequence Protein Precursors Eutherian mammals Peptide sequence hormones hormone substitutes and hormone antagonists medicine.drug |
| Zdroj: | International journal of peptide and protein research. 30(5) |
| ISSN: | 0367-8377 |
| Popis: | The neurohypophyseal hormones vasopressin and oxytocin are known to be synthesized in eutherian mammals as part of larger precursors containing either MSEL- or VLDV-neurophysins. A neurophysin has been isolated from ostrich neurohypophyses and shown by partial amino acid sequence determination to be related to mammalian VLDV-neurophysin. The present report describes the complete amino acid sequence of this ostrich neurophysin containing 93 residues. This amino acid sequence, the first reported in birds, differs in a remarkable manner from its mammalian homolog. Indeed, it contains a large number of substitutions, including one insertion, distributed throughout the polypeptide chain when compared to known VLDV-neurophysins. Whereas many of these substitutions are localized inside the so-called constant region of the neurophysin, the highest variation can be found in the COOH-terminal region. |
| Databáze: | OpenAIRE |
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