抄録
The venom of Agkistrodon halys bloemhoffii (Japaneses snake “Mamushi”) has two hemor-rhagic proteins, one of which is identical with proteinase b. Proteinase b was purified by column chromatography on anion exchange cellulose derivatives, sephadex and hydroxyl-apatite. The yield of purified proteinase b protein from lyophilized crude venom was 2.5 per cent. The purified preparation of this enzyme appeared to be chromatographically and electrophoretically homogeneous. The results of studies on the effect of heat treatment and inhibition by EDTA and cysteine, suggest that the hemorrhagic activity of the venom is due to the action of proteinase b. Moreover, the hemorrhagic and proteinase b activities could not be separated by chromatographical treatments. The purified proteinase b was an acidic protein and its sedimentation constant was calculated to be s20=4.82×10-13.
The authors express their thanks to Drs. T. Takagi and K. Kakiuchi of this Institute for the boundary electrophoresis and ultracentrifugal analysis.
