Characterization of two different peptides from the venom of the scorpion Buthus sindicus.
Two disulfide-rich, low-molecular mass peptides (approximately 3 kDa and approximately 4 kDa) have been isolated from Buthus sindicus venom using ion-exchange and reverse-phase HPLC. Peptide I has 35 residues with 8 half-cystine residues and is clearly related to four-disulfide core proteins of the neurophysin type and to toxins of other scorpion species (55-63% residue identity). Peptide II, present in low yield, has 28 residues with 6 half-cystine residues and a structure largely dissimilar from that of peptide I and other characterized toxins, although probably still a member of the disulfide core peptide type. Consequently, scorpion venom contains, in addition to toxins characterized before, toxin-like compounds with distant relationships.
Fazal
A
A
HEJ Research Institute of Chemistry, University of Karachi, Pakistan.
Beg
O U
OU
Shafqat
J
J
Zaidi
Z H
ZH
Jörnvall
H
H
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D012604:Scorpion Venoms / Q000032:analysis*
D010446:Peptide Fragments; D012604:Scorpion Venoms