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RISS 인기검색어
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- 저자 : 蔡奎宙 (검색결과 5 건)
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돼지 회충의 Sorbitol Dehydrogenase 에 관하여
채규주,이희성,이근배 ( Kyu Ju Chai,Hi Sung Lee,Keun Bai Lee ) 생화학분자생물학회 1978 BMB Reports Vol.11 No.4
The distribution of sorbitol dehydrogenase activity was studied in muscle, intestine and ovary of Ascaris strum. The tissues were fractionated by the method of Schneider and Hogeboom and the enzyme activity was measured using Gerlach and Hiby`s procedure. The results obtained were as follows: 1. The enzyme activity intrude preparations of muscle, intestine and ovary was found to be 1,152 units, 2,647 units and 3,366 units per g wet tissue, respectively. 2. Muscle showed the lowest enzyme activity among the tissues tested. Sventy-eight per cent of the activity was present in the cytosolic fraction(912 units/g wet weight). Twenty per cent of the activity (235 units/g wet tissue) was recovered in the mitochondria) fraction. 3. In the intestine, the activity was twice higher than that of muscle and 72% of the total activity was found in cytosolic fraction. 4. Ascaris ovary had the highest enzyme activity and contained 92% of the activity in the cytosolic fraction (3,400 units/g wet tissue).
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돼지 회충의 Sorbitol Dehydrogenase에 관하여
채규주,이희성,이근배,Chai, Kyu-Ju,Lee, Hi-Sung,Lee, Keun-Bai 생화학분자생물학회 1978 한국생화학회지 Vol.11 No.4
돼지회충(Ascaris suum)의 근육, 장관 및 난소조직을 분별 원심분리하여 핵, mitochondria 및 세포질을 분리하였으며, NAD 의존성인 sorbitol dehydrogenase의 활성도를 Gerlach and Hiby(1974)의 방법으로 측정하여 이 효소의 존재 유무 및 분포를 관찰하여 다음과 같은 결과를 얻었다. 1. 돼지회충의 근육, 장관 및 난소등의 조직 1g당 이 효소의 활성도는 각각 1152 unit, 2647 unit, 및 3666 unit 이다. 2. 근육조직의 세포질에는 79%인 912unit, mitochondria에는 20%인 235 unit 가 함유되어 있으며 비활성도는 3.84 및 3.56으로 작용능력은 거의 같다. 3. 장관조직에는 세포질에 72%인 1921 unit, mitochondria에는 13%인 352 unit 및 핵분획에 14%인 388 unit가 각각 함유되어 있다. 4. 난소조직에 이 효소가 가장 많이 함유되에 있으며, 92%인 3400 unit가 세포질에 함유되어 있으며 비활성도가 16.7로 이 효소의 작용능력이 다른 조직에 비하여 가장 활발하다. The distribution of sorbitol dehydrogenase activity was studied in muscle, intestine and ovary of Ascaris strum. The tissues were fractionated by the method of Schneider and Hogeboom and the enzyme activity was measured using Gerlach and Hiby's procedure. The results obtained were as follows: 1. The enzyme activity intrude preparations of muscle, intestine and ovary was found to be 1,152 units, 2,647 units and 3,366 units per g wet tissue, respectively. 2. Muscle showed the lowest enzyme activity among the tissues tested. Sventy-eight per cent of the activity was present in the cytosolic fraction(912 units/g wet weight). Twenty per cent of the activity (235 units/g wet tissue) was recovered in the mitochondria) fraction. 3. In the intestine, the activity was twice higher than that of muscle and 72% of the total activity was found in cytosolic fraction. 4. Ascaris ovary had the highest enzyme activity and contained 92% of the activity in the cytosolic fraction (3,400 units/g wet tissue).
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肝障害시 肝 및 血淸5' -NUCLEOTIDASE 活性의 變動
蔡奎周,高在景 한양대학교 의과대학 1982 한양의대 학술지 Vol.2 No.2
In order to evaluate mechanisms by which serum 5'-nucleotidase activity was increased in liver disorders, activities of 5'-nucleotidase bound to the membrane or solubilized by sodium dodecyl sulfate (SDS) were determined in homogenates and subcellular fractions of livers from rats treated with phenobarbital and CCl₄. Also measured was the activity of hepatic 5'-nucleotidase solubilized by SDS and separated by DEAE-cellulose chromatography in liver damaged rats, and the results were compared with those in normal rats. 1) Although the activity of serum 5'-nucleotidase was significantly increased in rats with hepatotoxicity induced by phenobarbital and CCl₄, the activity of the hepatic enzyme was not changed. These results indicate that the enzyme might be released from the damaged liver into the blood without showing any significant fall in the activity of the hepatic enzyme. 2) In Tris-and SDS-liver cell fractions (10³xg and 10⁴xg fractions) prepared from liver of rats with CCl₄ hepatotoxicity, ratio of 5'-nucleotidase a ciivity in the supernatant to that in the precipitates was observed to b increased as compared with that of normal rats. The result suggested that in rats with CCl₄ hepatotoxicity the activity of hepatic 5'-nucleotidase bound to the membrane was decreased and the activity of free or intermediated rom of the enzyme was increased. 3) The total actitity of hepatic 5'-nucleotidase separated by DEAE-cellulose chromato-graphy in rats with CCl₄ hepatotoxicity was greater than that in normal rats. This result confirmed that the activity of form of hepatic 5'-nucleotidase was increased in rats with CCl₄ hepatotoxicity. It can be concluded with the results obtained in the present study that an increase in the serum 5'-nucleotidase observed in rats with CCl₄ hepatotoxicity was due to the release into the blood of the free form of the enzyme that was found to be increased in the liver of rats with CCl₄hepatotoxicity.
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