1. Banded krait (
Bungarus multicinctus) venom was fractionated by zone electrophoresis into three fractions : one main protein fraction (2nd) with two minor (1 st and 3rd) protein fractions on both sides of it.
2. Although some toxic principles were detected in the 2nd protein fraction, the majority of the toxicity, representing 74.3 per cent of the recovered toxicity, was concentrated in the 1 st protein fraction.
3. All of the enzymes studied: phosphomonoesterase, phosphatidase A, cholinesterase, L-amino acid oxidase, and hyaluronidase activities were separated from the venom toxicity very distinctly, and were revealed as an electrophoretically single fraction just coinciding with the 3rd protein fraction.
4. Phosphodiesterase, 5'-nucleotidase, ATPase, DPN-pyrophosphatase, and proteinase activities in Banded krait venom were so feeble, hence they would not be a cause of venom toxicity.
5. It was definitely proved that the venom toxicity has nothing to do with any of enzyme activities studied, confirming our previous work.
The authors are gratefully indebted to Prof. R. Hirohata, chief of the Laboratory of Protein Chemistry, Yamaguchi Medical School, Ube, for his continued interest and encouragement during the course of this study.
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