Abstract
Crotoxin is the major toxin in the venom of the Brazilian rattlesnake (Crotulus &%~sus terrificus)‘. It is a complex of two subunits associated non-covalently: a basic protein (crotoxin PLA or crotoxin B) which carries the phospholipase (PLA) activity and an acidic protein (crotapotin or crotoxin A) which has no enzymic activity and is not toxic2,3. The lethal effect of crotoxin has been attributed to a pre-synaptic blockage of the neuromuscular transmission 4, but it has been shown that the toxin acts also at the post-synaptic level 5,6. Habermann and Breithaupt’ stated that the separation of these two subunits was one of the three important goals in the study of crotoxin. In previous reports, these two subunits were separated after alkylation or acylation of the amino groups*, on a carboxymethylcellulose column at pH 4 or on a DEAE-cellulose column in 6 M urea 2,3,g. More recently, two subunits of human pituitary thyrotropin and pike eel gonadotropin have been successfully separated by hydrophobic interaction chromatography l”,ll. Judging from the amino acid compositions12, the two subunits of crotoxin have a large difference in hydrophobicity and thus may be separated by reversed-phase liquid chromatography. In this work the separation of the two subunits of crotoxin by high-performance liquid chromatography (HPLC) was investigated, and an unexpected finding is reported.
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