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J. Biochem, 1968, Vol. 64, No. 2 215-225
© 1968 Japanese Biochemical Society

research-article

Studies on Snake Venoms

XVIII. An Improved Method for Purification of the Proteinase b from the Venom of Agkistrodon halys blomhoffii and Its Physicochemical Properteis*,**

GENICHIRO OSHIMA, SADAAKI IWAGANA and TOMOJI SUZUKI

From the Institute for Protein Research, Osaka University, Kita-ku, Osaka

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.

* XVII. S. Iwanaga, T. Sato, Y. Mizushima, and T. Suzuki, J. Biochem., 58, 123 (1965).

**A part of this paper was reported at the 38th General Meeting of the Japanease Biochemical Society(1965). This work was supported by a grant from the Ministry of Education, Japan and by a grant from Toyo Rayon Foundation for the Promotion of Science and Technology


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