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J. Biol. Chem., Vol. 259, Issue 19, 11751-11755, Oct, 1984
DS Parker, JP Raufman, TL O'Donohue, M Bledsoe, H Yoshida and JJ Pisano
The amino acid sequences of two closely related peptides from Gila monster
(Heloderma suspectum) venom are reported. Helospectin I is a 38- residue
peptide, His-Ser-Asp-Ala-Thr-Phe-Thr-Ala-Glu-Tyr-Ser-Lys-Leu-
Leu-Ala-Lys-Leu-Ala- Leu-Gln - Lys-Tyr-Leu-Glu-Ser-Ile-Leu-Gly-Ser-Ser-
Thr-Ser-Pro-Arg-Pro-Pro-Ser-Ser, and helospectin II is a 37-residue peptide
identical to helospectin I except that it lacks serine 38. Helospectins are
pancreatic secretagogues with structures and bioactivities similar to
vasoactive intestinal peptide and other members of the glucagon
superfamily. The relative significance of helospectin-I and helospectin-II
is presently unknown. Comparison of the 28 residues of vasoactive
intestinal peptide with residues 1-28 of helospectin shows that identical
amino acids occur in 15 positions. Since members of the glucagon
superfamily have similar structures but different biological actions, it is
possible that helospectin is more closely related to a mammalian peptide
awaiting discovery.
Amino acid sequences of helospectins, new members of the glucagon superfamily, found in Gila monster venom
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