scholarly journals Purification and chemical characterization of the major toxins from the venom of the Brazilian scorpion Tityus serrulatus Lutz and Mello

1981 ◽  
Vol 46 (4) ◽  
pp. 195-205 ◽  
Author(s):  
Lourival Domingos Possani ◽  
Brian M. Martin ◽  
Javier Mochca-Morales ◽  
Ib Svendsen
1996 ◽  
Vol 313 (3) ◽  
pp. 753-760 ◽  
Author(s):  
Baltazar BECERRIL ◽  
Miguel CORONA ◽  
Fredy I. V. CORONAS ◽  
Fernando ZAMUDIO ◽  
Emma S. CALDERONARANDA ◽  
...  

Seven toxic peptides from the venom of Tityus bahiensis and Tityus stigmurus were isolated and sequenced, five of them to completion. The most abundant peptide from each of these two species of scorpion was 95% identical with that of toxin γ from the venom of Tityus serrulatus. They were consequently named γ-b and γ-st respectively. The genes encoding these new γ-like peptides were cloned and sequenced by utilizing oligonucleotides synthesized according to known cDNA sequences of toxin γ, and amplified by PCR on templates of DNA purified from both T. bahiensis and T. stigmurus. They contain an intron of approx. 470 bp. Possible mechanisms of processing and expressing these peptides are discussed, in view of the fact that glycine is the first residue of the N-terminal sequence of T. stigmurus, whereas lysine is the residue at position 1 of toxin γ from T. serrulatus and T. bahiensis. In addition, chemical characterization of the less abundant toxic peptides showed the presence of at least four distinct families of peptides in all three species of the genus Tityus studied. There is a large degree of similarity among peptides from different venoms of the same family. By using specific horse and rabbit antisera, the venoms of T. bahiensis, T. serrulatus and T. stigmurus were compared. They showed an extended degree of cross-reactivity. Thus these three species of scorpion have similar toxic components, the genes of which are similarly organized, processed and expressed.


1981 ◽  
Author(s):  
Birgitta Berglund ◽  
Ulf Berglund ◽  
Thomas Lindvall ◽  
Helene Nicander-Bredberg

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.


Alergologia ◽  
2020 ◽  
Vol 1 (4) ◽  
pp. 7
Author(s):  
Mariana Vieru ◽  
Florin-Dan Popescu ◽  
Laura Haidar ◽  
Carmen Bunu-Panaitescu

2010 ◽  
Vol 35 (5) ◽  
pp. 261-267 ◽  
Author(s):  
Wissemn Gallala ◽  
Mohamed Essghaier Gaied ◽  
Borhen Kchaou

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