par Hoshino, Minoru;Yanaihara, Chizuko;Hong, Yeong Man;Kishida, Satoshi;Katsumaru, Yumiko;Vandermeers, André ;Vandermeers-Piret, Marie-Claire ;Robberecht, Patrick ;Christophe, Jean ;Yanaihara, Noboru
Référence FEBS letters, 178, 2, page (233-239)
Publication Publié, 1984-12
Référence FEBS letters, 178, 2, page (233-239)
Publication Publié, 1984-12
Article révisé par les pairs
Résumé : | 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. |