Abstract
The crude liver extract of rabbit had the hydrolyzing activity for ascorbate 2-sulfate (AsS) and gave inorganic sulfate with L-ascorbic acid (AsA). The optimum pH of this crude enzyme was 4.0 (sodium acetate buffer). The extracts from some organs of guinea pig and trout liver also had the hydrolyzing activity. When the enzyme activity in the livers of these animals were compared, those of the rabbit and the guinea pig were higher than that of the trout. Among the liver, adrenals, kidney, spleen and intestine of the guinea pig, the adrenals gave the highest specific activity, which was about 30 times higher than that of the liver. The purification of the crude enzyme from the rabbit liver was carried out using by ammonium sulfate or aceton precipitation method. The precipitate under 40% saturation of ammonium sulfate showed a specific activity about 4 times higher than that of the crude extract. On the other hand, the activity of the fraction from 40 to 50% concentration of aceton was only about 2 times higher than that of the crude extract.
