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해녀콩 ( Canavalia Iineata ) 자엽에서 Homoserine Dehydrogenase 의 정제 및 특성
이주용(Ju Yong Lee),이이(Yi Lee),권영명(Young Myung Kwon) 한국식물학회 1996 Journal of Plant Biology Vol.39 No.1
Two forms of homoserine dehydrogenase have been isolated from 8-day-old cotyledons of Canavalia lineata by a heat denaturation, ammonium sulfate fractionation, DEAE-Sephacelion exchange and Sephacryl S-300 gel filtration chromatographies, and Procion red dye, Cibacron blue dye and Resource Q column chromatographies. The molecular weights of T-form(threonine-sensitive) and K-form(threonine- insensitive) were estimated to 230 kD and 135 kD, respectively. In the presence of 10 mM threonine, the activity of T-form was inhibited with almost 70%, but that of K-form was not at all. The Km values for homoserine of T- and K- form were 1.6 mM and 0.3 mM, respectively. The Km values for NAD of T- and K-form were 2.34 mM and 0.03 mM, respectively. And Km values for NADP of two isozymes were the same as 0.01 mM. The activities of T- and K-form were markedly stimulated up to 4.9- and 2.8-fold, respectively, by 400 mM KCI. The partial purified(gel filtration) enzymes(T-form and K-form) can be reversibly converted.
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Rhizobium sp . SNU 003 의 생육에 미치는 Canavanine 과 Arginine 의 영향 및 Arginine Deiminase 의 성질
이주용,권영명 ( Ju Yong Lee,Young Myung Kwon ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.2
The growth of Rhizobium sp. SNU 003 isolated from the nodule of Canavalia lineata was inhibited by canavanine and promoted by arginine. The growth inhibited by 2 mM canavanine was approximately shown 78-95% recovery by the addition of 2-20 mM arginine. Arginine deiminase of this Rhizobhtm is an active catabolic enzyme of arginine and the enzyme activity was promoted about 10-times when arginine was added into the medium. Arginine deiminase was purified 45-fold and the yield was 11% by the following steps: Protamine sulfate and ammonium sulfate precipitation, DEAE-Sephacel chromatography, and Sephacryl S-300 gel chromatography. The molecular weight of the native enzyme was 190,000 by gel filtration and optimum temperature for activity was 30℃. Enzyme showed the highest activity at pH 6.0 in the sodium-acetate buffer. Canavanine was not catabolized by arginine deiminase and competitively inhibited the degradation of arginine. The activity of enzyme was inhibited by Co^(2+), A1^(3+), Cu^(2+), Pb^(2+) and Zn^(2+), however promoted by 1() mM of Mg^(2+) and Mn^(2+) approximately 30-40%.
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해녀콩 캘러스에서 pH 변화에 따른 Arginase 의 활성
이주용(Ju Yong Lee),김상구(Sang Gu Kim),권영명(Young Myung Kwon) 한국식물학회 1993 Journal of Plant Biology Vol.36 No.4
As callus from Canavalia lineata L. (DC) was treated in pH8 buffer solution for one hour, arginase activity in its cell free extracts was twice higher than in pH 6. From the cell free extracts, two forms of arginase, heavy and light, were appeared in Sephacryl S-200 gel filtration. One form of arginase (heavy form) was estimated in 380 kD and another form (light form) was 179 kD in Sephacryle S-300 column chromatography. The heavy form at pH 8 and light form at pH 6 were predominant, respectively. However, even at pH 6 the heavy form was mainly appeared by the addition of 0.5 mM Mn^2+ in the cellus floating solution. And the light form from the column was easily transformed into the heavy form in pH 8. Arginase activity of light form was increased to about same value of heavy form by the incubation with Mn^2+ for 30 min in vitro, but heavy form did not showed any increasment in its cataltic activity with additional Mn^2+. In condition of Mn^2+ free assay system, K_m and V_max was estimated in 22 mM and 1.61 μmole urea·min^-1·mg^-1 protein of heavy form, and 30 mM and 0.79 μmole urea·min^-1·mg^-1 protein of light form at pH 9.7.
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Rhizobium sp. SNU 003의 생육에 미치는 Canavanine과 Arginine의 영향 및 Arginine Deiminase의 성질
이주용,권영명,Lee, Ju-Yong,Kwon, Youn-Myung 생화학분자생물학회 1990 한국생화학회지 Vol.23 No.2
해녀콩(Canavalia lineata)의 뿌리에서 분리한 Rhizobium sp. SNU 003은 arginine에 의해서는 생육이 촉진되나 canavanine에 의해서는 생육이 억제된다. 또한 2mM의 canavanine에 의해 억제된 생육은 2~20 mM의 arginine 첨가에 의해 약 78~95%의 회복을 보여주었다. Rhizobium에서 arginine의 대사는 arginine deiminase의 작용으로 시작되며, arginine의 존재로 이 효소의 활성은 약 10배 증가하였다. Arginine deiminase는 protamine sulfate에 의한 침전, DEAE-Sephacel 이온교환 크로마토그래피와 Sephacryl S-300 gel 크로마토그래피에 의하여 45배로 정제되었으며, 회수율은 11%였다. Sephacryl S-300 gel 컬럼 크로마토그래피로 분자량은 190,000임을 알았다. Sodiumacetate 완충용액에서의 활성 최적온도는 $30^{\circ}C$, 최적 pH는 6.0으로 밝혀졌다. Canavanine은 기질로서 이용될 수 없으며, arginine의 이용을 경쟁적으로 억제하였다. 효소의 활성은 $Co^{2+}$, $Al^{3+}$, $Pb^{2+}$ 및 $Zn^{2+}$에 의해서는 억제되었으나, 10 mM의 $Mg^{2+}$와 $Mn^{2+}$에 의해서는 30~40% 증가하였다. The growth of Rhizobium sp. SNU 003 isolated from the nodule of Canaialia lineata was inhibited by canavanine and promoted by arginine. The growth inhibited by 2 mM canavanine was approximately shown 78 - 95% recovery by the addition of 2 - 20 mM arginine. Arginine deiminase of this Rhizobium is an active catabolic enzyme of arginine and the enzyme activity was promoted about 10-times when arginine was added into the medium. Arginine deminase was purified 45-fold and the yield was 11% by the following steps: Protamine sulfate and ammonium sulfate precipitation, DEAE-Sephacel chromatography, and Sephacryl S-300 gel chromatography. The molecular weight of the native enzyme was 190,000 by gel filtration and optimum temperature for activity was $30^{\circ}C$. Enzyme showed the highest activity at pH 6.0 in the sodium-acetate buffer. Canavanine was not catabolized by arginine deiminase and competitively inhibited the degradation of arginine. The activity of enzyme was inhibited by $Co^{2+}$, $Al^{3+}$, $Cu^{2+}$, $Pb^{2+}$ and $Zn^{2+}$, however promoted by 10 mM of $Mg^{2+}$ and $Mn^{2+}$ approximately 30 - 40%.
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