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J. Biochem, 1968, Vol. 64, No. 2 227-238
© 1968 Japanese Biochemical Society

research-article

Studies on Snake Venoms*

XIX. Purification and Some Physicochemical Properties of Proteinases a and c from the Venom of Agkistrodon halys blomhoffii,**

GENICHIRO OSHIMA, YUSHI MATSUO, SADAAKI IWANAOA and TOMOJI SUZUKI

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

1. Proteinases a and c from the venom of A. halys blomhoffii have been purified by successive use of ion-exchange chromatography and gel filtration. From 32.7 g of the lyophilized venom 138 mg of purified proteinase a and 2.69 g of purified proteinase c were obtained. The purified preparations of proteinases a and c are essentially homogeneous as observed by sedimentation in the ultracentrifuge, free-boundary ele-ctrophoresis and column chromatography.

2. The values of the sedimentation constants extrapolated to zero concentration, s20{ring}, w, are 3.63 S and 4.94 S for proteinase a and c, respectively. The diffusion constant for proteinase c, D{ring}20o w, is 5.88 × 10–7cm2 sec–1. The partial specific volume of proteinase c, D{ring}20, w, is 0.695 ml/g and its intrinsic viscosity, [n], is 0.046 dl/g. The molecular weights of proteinases a and c are computed to be about 50,000 for the former and about 70,000 for the latter. Free-boundary electrophoreses give isoelectric points of pH 6.0 for proteinase a and 3.85 for proteinase c. Their absorbancies A1%1cm at 280 mµ, are 9.08 and 10.98 for proteinases a and c, respectively. Their contents of nitrogen are 13.83 and 13.90 per cent and those of polypeptides 76.5 and 91.2 per cent for proteinases a and c, respectively.

3. Both proteinases a and c contain sugars in their molecules, 13.6 per cent for the former and 8.46 per cent for the latter.

*XVIII. G. Oshima, S. Iwanaga, and T. Suzuki, J. Biochem., 64, 215 (1968).

** A part of this paper was reported at the 38th General Meeting of the Japanese 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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