Open AccessSnake Venom Toxins
Author(s) -
JOUBERT François J.
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10291.x
Subject(s) - edman degradation , venom , toxin , chromatography , sephadex , chemistry , trypsin , size exclusion chromatography , ion chromatography , peptide sequence , biochemistry , aristolochic acid , biology , enzyme , genetics , gene
Three toxins (CM‐8, CM‐11, and CM‐13a) were purified from the venom of Naja haje annulifera by gel filtration on Sephadex G‐50 and by ion‐exchange chromatography on CM‐cellulose. Whereas toxin CM‐8 and CM‐11 comprise 60 amino acid residues, toxin CM‐13a contains 61 residues. All three toxins are cross‐linked by four intrachain disulphide bridges. The complete amino acid sequences of these toxins have been elucidated. The reduced and S‐carboxymethylated toxins were digested with trypsin and chymotrypsin and the peptides purified by ion‐exchange chromatography, gel filtration and chromatography or electrophoresis on paper. The Edman procedure, either through the use of the automatic sequencer or by manual manipulation, was employed to obtain the sequence of the intact toxins and the pure peptides. The chymotryptic digests provided the necessary overlapping peptides which allowed the alignment of the tryptic peptides. The properties of the three toxins were compared with those of the cytotoxin group. The toxicities the serological properties, the sequences and the invariant amino acid residues of toxin CM‐8 and CM‐11 resemble the corresponding properties of the cytotoxin group. The sequence and serological properties of toxin CM‐13a show that it is related to the cytotoxin group, but its toxicity is much lower than those encountered in the cytotoxin group.