Characterization of two different peptides from the venom of the scorpion Buthus sindicus
- 6 November 1989
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 257 (2) , 260-262
- https://doi.org/10.1016/0014-5793(89)81548-0
Abstract
Two disulfide-rich, low-molecular mass peptides (~3 kDa and ~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.Keywords
This publication has 10 references indexed in Scilit:
- Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymesBiochemistry, 1988
- Structure of a heat‐stable enterotoxin produced by a human strain of Escherichia coliFEBS Letters, 1983
- Covalent structure of the insect toxin of : Hervé DARBON, Hervé ROCHAT, Charles KOPEYAN, Jurphaas VAN RIETSCHOTEN and Eliahu ZLOTKIN Laboratoire de Biochimie, Faculté de Médecine Secteur Nord, Bd. P. Dramard, 13326 Marseille Cedex 3. Department of Zoology, The Hebrew University of Jerusalem, IsraëlToxicon, 1982
- Insect toxic component from the venom of a chactoid scorpion, Scorpio maurus palmatus (Scorpionidae).Journal of Biological Chemistry, 1982
- The structure of neurophysin.Published by Elsevier ,1981
- Three-dimensional structure of a protein from scorpion venom: a new structural class of neurotoxins.Proceedings of the National Academy of Sciences, 1980
- The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core.Journal of Biological Chemistry, 1980
- Neurotoxins that Act on Voltage-Sensitive Sodium Channels in Excitable MembranesAnnual Review of Pharmacology and Toxicology, 1980
- Micro‐sequence analysis of peptides and proteins using 4‐NN‐dimethylaminoazobenzene 4′‐isothiocyanate/phenylisothiocyanate double coupling methodFEBS Letters, 1978
- Purification and partial characterization of a second toxin from the scorpion Tityus serrulatusComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1976