Primary structure of helodermin, a VIP‐secretin‐like peptide isolated from Gila monster venom
- 10 December 1984
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 178 (2) , 233-239
- https://doi.org/10.1016/0014-5793(84)80607-9
Abstract
The complete amino acid sequence of helodermin isolated from the venom of Gila monster was elucidated. The peptide was shown to be a basic pentatriacontapeptide amide: His-Ser-Asp-Ala-Ile-Phe-Thr-Gln-Gln- Tyr-Ser-Lys-Leu-Leu-Ala-Lys-Leu-Ala-Leu-Gln-Lys-Tyr-Leu-Ala-Ser-Ile-Leu-Gly-Ser-Arg-Thr-Ser-Pro-Pro-Pro-NH2. A high degree of sequence similarities to secretin/VIP/PHI/(PHM)/GRF from mammal and bird was observed over the entire N-terminal 1-27 sequence. In particular, the amino acid residues in positions 3, 6 and 7 were found to be common to 9 peptides of the family. Another interesting feature of the structure of helodermin was its C-terminal -Pro-Pro-Pro-NH2 sequence. Isolation of helodermin was the first demonstration of the existence of a secretin/VIP-related peptide in an animal that is neither mammal nor bird. © 1984.SCOPUS: ar.jinfo:eu-repo/semantics/publisheKeywords
This publication has 6 references indexed in Scilit:
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