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Identification Of Horse Antivenom Reactivity Against Egyptian Elapidae Venom Proteins By Two-Dimensional Gel-Electrophoresis.

EL-Rashdy M. Redwan

Protein Research Department, GEBRI, Mubarak City for Scientific Research and Technological Application, New Borg El-Arab, Alexandria, Egypt.

The importance of characterizing venom proteins from the Egyptian elapidae, especifically neurotoxins, is based on the need to produce an effective antivenom. Two-dimensional gel electrophoresis was used to separate and identify cobra venom proteins. About 30-50 distinct protein spots were identified on silver stained two dimensional gels. Two-thirds of the venom proteins displayed anionic migration and low molecular weight. The venoms from Naja haja and Naja nigricollus showed 45-50 spots, while Walternnesia aegyptia had 30-35 spots. VACSERA polyclonal anti-venom had a strong signal for anionic and cationic venom protein spots with molecular weight <115 kDa. However, it showed weak or no reactivity toward anionic low molecular weight spots (3-15kDa). These results suggest the need to change the horse immunization regime to include low molecular weight neurotoxin proteins.