Primary structure of helodermin, a VIP-secretin-like peptide isolated from Gila monster venom

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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.

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APA

Hoshino, M., Yanaihara, C., Hong, Y. M., Kishida, S., Katsumaru, Y., Vandermeers, A., … Yanaihara, N. (1984). Primary structure of helodermin, a VIP-secretin-like peptide isolated from Gila monster venom. FEBS Letters, 178(2), 233–239. https://doi.org/10.1016/0014-5793(84)80607-9

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