Abstract
A polypeptide was purified from frog brain extracts on the basis of its ability to inhibit α-melanotropin release from perifused frog neurointermediate lobes. Based on Edman degradation, amino acid analysis, and peptide mapping, the primary structure of this frog melanotropin-release-inhibiting factor (melanostatin) was determined to be H-TyrPro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-Glu-Asp-Met-Ala-Lys- Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg-Gln-Arg-Tyr-NH 2. Frog melanostatin belongs to the pancreatic polypeptide/neuropeptide Y/peptide YY family, and the structure of this peptide differs from that of human neuropeptide Y by only one amino acid substitution in position 19. A synthetic replicate of frog melanostatin is coeluted with the native peptide on HPLC and is highly potent in inhibiting α-melanotropin secretion in vitro (IC50 = 60 nM).
Original language | English |
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Pages (from-to) | 3862-3866 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 88 |
Issue number | 9 |
Publication status | Published (in print/issue) - 1991 |
Keywords
- Control of pigmentation
- Evolution
- Peptide isolation
- Peptide mapping
- Pituitary melanotrophs