| Literature DB >> 6439576 |
M Hoshino, C Yanaihara, Y M Hong, S Kishida, Y Katsumaru, A Vandermeers, M C Vandermeers-Piret, P Robberecht, J Christophe, N Yanaihara.
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.Entities:
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Year: 1984 PMID： 6439576 DOI： 10.1016/0014-5793(84)80607-9
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124