Studies on Snake Venoms

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Abstract
1. Lots of proteinase b, one of the two hemorrhagic proteins in the venom of Agkistrodon halys blomhoffii, were prepared by the modified methods using a column chromatography on DEAE-cellulose and a gel filtration on Sephadex G-100. The preparation obtained was homogeneous in ultracentrifugation, in free boundary electrophoresis and on column chromatographies. 2. Sedimentation and diffusion constants of proteinase b were 5.54 S, and 5.26 × 10−7cm2/sec, respectively, and its molecular weight was found to be about 95, 000. Its isoelectric point was pH 4.18. The mobility at pH 8.51 for the descending pattern was 5.82×10−5 cm2/sec volt. 3. The content of aspartic acid was 12.5 per cent and this value was higher than those of usual proteins. Chemical compositions of proteinase b were as follows: nitrogen 12.4 per cent, polypeptide moiety 76.5 per cent, neutral sugars (galactose, mannose and trace of fucose) 8 per cent, glucosamine 6.5 per cent, and sialic acid 3 per cent. Thus, the venom proteinase b was characterized to be a glycoprotein.

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