Biochemical and Antigenic Properties of a Purified Neurotoxin of Vipera Palestinae Venom

Open Access
Publisher Website
Google Scholar
Abstract
Summary: The various activities—neurotoxic, proteolytic and anticoagulant—contained in the DEAE cellulose neurotoxic fraction of Vipera palestinae venom can be adequately separated by means of ammonium sulfate fractionation. The recovery of the neurotoxin, free from protease(s) and anticoagulant, is in the vicinity of 35%. Electrophoretic analysis of the isolated neurotoxin shows three different fractions, of which only one, positively charged, has lethal activity in mice. This component produces a single precipitation line in an agar immune electrophoresis plate. Venom protease(s), free of neurotoxic and anticoagulant activity, enhance the lethal activity of neurotoxin. The nondialyzable neurotoxin is split by trypsin and the dialysate is toxic for mice. Up to 1400 LD50 of the purified neurotoxin may be bound to and detoxified by 1 g of carboxymethyl cellulose (CMC). The CMC-bound isolated neurotoxin is highly immunogenic in rabbits.