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Purification and sequence determination of a new muscarinic toxin (MT4) from the venom of the greem mamba (Dendroaspis angusticeps)

par Vandermeers, André ;Vandermeers-Piret, Marie-Claire ;Rathe, Jean ;Waelbroeck, Magali ;Jolkkonen, Mikael;Oras, Aldo;Karlsson, Evert
Référence Toxicon, 33, 9, page (1171-1179)
Publication Publié, 1995

Article révisé par les pairs

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Résumé :

A toxin which partially inhibited [3H]N-methylscopolamine binding to rat brain muscarinic receptors was purified from the venom of green mamba, Dendroaspis angusticeps. The N-terminal sequence (up to 45 amino acids) was determined by automated Edman degradation of the whole molecule. The complete sequence was elucidated after enzymatic cleavage with endoproteinase Arg-C or endoproteinase lys-C and peptide fragments purification. The identity of the C-terminal amino acid was confirmed by hydrazinolysis. The new toxin (MT4) had eight half-cystines and 66 amino acids. It differed from muscarinic toxin MT1 by a single substitution in position 57 (arginine in MT1, histidine in MT4), proximal to the sixth half-cystine.