1) 조효소액(粗酵素液)을 유안염석(硫安鹽析)(0.5포화도(飽和度)) Sephadex G 25에 의(依)한 제염(除鹽), CM Cellulose column chromatography, Sephadex G 25에 의(依)한 농축(濃縮), Sephadex G 75 gel filtration에 의(依)하여 Specific activity 126.5/mg protein, 원활성(原活性)의 약(約) 45배(倍), 수율(收率) 4.2%의 정제효소(精製酵素)를 얻었다. 2) 정제효소(精製酵素)를 Acrylamide gel disc electrophoresis에 의(依)하여 분리(分離)시킨 결과(結果) 하나의 주(主)된 band와 그 양측(兩側)에 2개(個)의 희미한 band가 나타나 있으므로 하나의 순수(純粹)한 단백질(蛋白質)이라고는 할 수 없으나 조효소액(粗酵素液)에 비(比)하여 상당(相當)히 정제(精製)되었다.
1) The purified enzyme was obtained with the specific activity 126.5 u/mg protein (about 45 times of the original activity) and the yield of 4.2%, by means of salting out with ammonium sulfate (0.5 saturation) of the crude enzyme solution, desalting by Sephadex G 25, CM cellulose columm chromatography, concentration by Sephadex G 25, and gel filtration by Sephadex G 75. 2) In the acrylamide gel disc electrophoresis of the purified enzyme, the main band and two obscure ones on the both side of the main band appeared, which indicated that the enzyme was considerably purified compared with its crude enzyme solution, even if it is not referred to as a pure protein.
