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- 검색키워드
- 저자 : 조성희 ( Dong Wook Lee (검색결과 3 건)
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이동욱,이희성,조성희,Lee, Dong-Wook,Lee, Hee-Sung,Cho, Sung-Hye 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.3
흰쥐 신장의 NAD 의존성 ${\alpha}$-glycerophosphate 탈수소 효소는 4종의 isozyme으로 존재하였고 그들의 등전점은 pH6.9, 6.6, 6.4 및 6.2였다. 이들중 등전점 6.6인 major isozyme을 blue dextran-Sepharose 4B, DEAE-cellulose, Sephadex G-100 chromatography를 통하여 1,078배 정제하였다. Major isozyme의 분자량은 62,000이고, 반응 최적온도와 pH는 각각 55도 및 10.0이었고, 최적온도에서 쉽게 불활성화 되었다. 이 효소는 일가 및 이가 양이온의 첨가에 의해 활성화 되었으며 p-HMB와 iodoacetamide에 의해 활성이 크게 억제되었고, glycerophosphate와 NAD에 대한 Km값은 각각 3.22 및 0.31 mM 이었다. 이들 결과로부터 이 효소의 isozyme pattern은 조직에 따라 다를지라도 major isozyme의 이화학적 성상은 서로 비슷함을 알 수 있었다. NAD-linked ${\alpha}$-glycerophosphate dehydrogenase(EC 1.1.1.8) in rat kidney existed as four different isozymic forms with an isoelectric point at pH 6.9, 6.6, 6.4 and 6.2, respectively. The major isozymic form(PI 6.6) was purified using several chromatographic procedures involving an ion exchange and two affinity chromatography steps. The 1,078 fold purified enzyme was homogeneous, nucleotide free protein. The molecular weight of the major isozyme was 62,000 daltons, the optimal pH and temperature for its catalytic activity were 10.0 and $55^{\circ}C$, respectively. At the optimal temperature this enzyme was rapidly inactivated$(t_{1/2}=1.5min)$. The major isozyme was activated by the addition of cations such as $K^+$, $Na^+$, $Mg^{++}$ or $Ca^{++}$, and was strongly inhibited by alkylating agents such as P-hydroxymercurybenzoate or iodoacetamide. Glycerophosphate oxidation reaction obeyed the Michaelis-Menton behavior with Km values of 3.22 and 0.31 mM for glycerophosphate and NAD, respectively. The data suggest that although the isozyme pattern of NAD-linked ${\alpha}$-glycerophosphate dehydrogenase is quite different by tissue or species of the animal the physico-chemical properties of the major isozymic form are very similar each other except the affinity for substrate and coenzyme.
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소나무 꽃가루에서 분리한 Trehalase의 정제 및 성상에 관한 연구
이동욱,이희성,조성희,Lee, Dong-Wook,Lee, Hi-Sung,Cho, Sung-Hee 생화학분자생물학회 1981 한국생화학회지 Vol.14 No.2
소나무 꽃가루를 파쇄하여 Hogeboom (1968)의 방법으로 세포의 각 분획을 분리하였다. 그리고 trehalase의 활성도를 측정하고 세포질 분획의 trehalase 를 ammonium sulfate에 의한 침전, DEAE-cellulose 및 Sephadex G-200 column chromatography를 행하여 정제하였으며 그 성상을 관찰하여 다음과 같은 결론을 얻었다. 1. 소나무 꽃가루에 있는 trehalase 는 cytosol에 약 80% 그리고 mitochondria에 약 4%, nuclei 에 약 10% 함유되어 있었다. 2. 소나무 꽃가루의 세포질 분획에서 이 효소를 81배 정제하였으며, 기질로는 trehalose에 대해서만 활성을 나타냈다. 3. 이 효소활성의 최적 pH 는 5.4였으며, 최적온도는 $60^{\circ}C$였다. 4. 이 효소의 기질에 대한 Km값은 $2.56{\times}10^{-3}M$이었다. 5. 반응 생성물이 glucose임을 paper chromatography에 의해 확인하였다. 6. 양이온이 이 효소에 미치는 영향은 $Na^+$이 $1{\times}10^{-4}{\sim}1{\times}10^{-3}M$농도에서 효소활성도를 약 14~17% 증가시켰으나, 농도의 증가에 따라 억제 현상이 증가되었다. 또 $Mg^{++}$ 경우에도 $1{\times}10^{-5}M{\sim}1{\times}10^{-4}M$ 농도에서 활성도가 27~15% 증가되었으나 농도의 증가에 따라 현저한 억제현상을 보였다. 7. $K^+$, $Ca^{++}$의 경우에는 같은 농도 범위에서 효소활성에 변화가 없었다. 8. 이 효소의 분자량은 약 70,000이었다. Trehalose, the alpha-1,1 linked disaccharide of glucose, occurs widely in nature. This sugar has been isolated from bacteria, yeast, fungi and a number of invertebrates, where it functions as reserve carbohydrate. Trehalase(${\alpha},{\alpha}$-trehalose 1-D-glucohydrolase, EC 3.2.1.28.) responsible for the hydrolysis of trehalose was isolated from pine pollen(Pinus densiflora Siebold) and purified 81 times by DEAE-cellulose column and Sephadex G-200 column chromatography. The activity of trehalase was measured by method of Lapp and Mason. The enzyme activity in pine pollen was detected 80.46% in cytosolic fraction, 4.09% in mitochondria) fraction and 10.33% in nucleic fraction. The pH optimum for enzymatic activity was found to be 5.4 and optimal temperature was $60^{\circ}C$ and the Km value for trehalose was estimated to be about $2. 56{\times}10^{-3}M$. The product of reaction was identited as D-glucose by paper chromatographic method. The trehalase activity was activated as much as 14∼17% by $1{\times}10^{-4}M{\sim}1{\times}10^{-3}M$ concentration of $Na^+$, and 27~15% by $1{\times}10^{-5}M{\sim}1{\times}10^{-4}M$ of $Mg^{++}$, and the other cations($K^+$, $Ca^{++}$) were tested for their abillity to replace $Mg^{++}$, but none was effective. The molecular weight of trehalase was estimated to be approximately 70,000 by Sephadex G-200 gel filtration.
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소나무 꽃가루에서 분리한 Trehalase 의 정제 및 성상에 관한 연구
이동욱,이희성,조성희 ( Dong Wook Lee,Hi Sung Lee,Sung Hee Cho ) 생화학분자생물학회 1981 BMB Reports Vol.14 No.2
Trehalose, the alpha-1, 1 linked disaccharide of glucose, occurs widely in nature. This sugar has been isolated from bacteria, yeast, fungi and a number of invertebrates, where it functions as reserve carbohydrate. Trehalase(α,α-trehalose 1-D-glucohydrolase, EC 3. 2. 1. 28. ) responsible for the hydrolysis of trehalose was isolated from pine pollen(Pinus densiflora Siebold) and purified 81 times by DEAE-cellulose column and Sephadex G-200 column chromatography. The activity of trehalase was measured by method of Lapp and Mason. The enzyme activity in pine pollen was detected 80.46% in cytosolic fraction, 4.09% in mitochondria) fraction and 10.33% in nucleic fraction. The pH optimum for enzymatic activity was found to be 5.4 and optimal temperature was 60℃ and the Km value for trehalose was estimated to be about 2. 56 × 10^(-3)M. The product of reaction was identited as D-glucose by paper chromatographic method. The trehalase activity was activated as much as 14∼17% by 1 × 10^(-4)M∼1 × 10^(-3)M concentration of Na^+, and 27∼15% by 1 × 10^(-5)∼1 × 10^(-4)M of Mg^(++), and the other cations(K+, Ca++) were tested for their abillity to replace Mg^(++), but none was effective. The molecular weight of trehalase was estimated to be approximately 70,000 by Sephadex G-200 gel filtration.
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