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RISS 인기검색어
- 검색키워드
- 저자 : 김유삼 ( Jin Kyu Park (검색결과 2 건)
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- 유료
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Isolation and Characterization of an Extracellular p-Nitrophenylacetate Hydrolase from Pine
박진규,김유삼,Park, Jin-Kyu,Kim, Yu-Sam 생화학분자생물학회 1983 한국생화학회지 Vol.16 No.3
p-Nitrophenylacetate hydrolase was detected in the extracellular fluid of pine pollen and purified by the combination of DEAE cellulose ion exchange chromatography and Sephadex G-100 gel filtration. The purification steps resulted in about 59 fold purification with 37% recovery of the enzyme activity. The purified enzyme showed a single protein band on the acrylamide gel after electrophoresis and the molecular weight of the enzyme was estimated to be 47,000 dalton by gel filtration with a calibrated Sephadex G-100 column. Its enzyme activity was inhibited by a thiol-directed reagent, p-chloromercuribenzene sulfonic acid. The optimum pH of this enzyme was 8.0 and a typical Michelis-Menten type saturation pattern with increasing concentration of p-Nitrophenylacetate was obtained. From the double reciprocal plot its Km value was calculated to be $166\;{\mu}M$. This enzyme also hydrolyzed p-nitrophenylacetate but not tripalmitin. 송화가루의 추출물로부터 p-nitrophenylacetate를 분해 하는 효소(PNA hydrolase)를 검정하고 이 효소를 DEAE cellulose ion exchange chromatography와 Sephadex G-100 gel filtration을 통하여 정제하였다. 정제효소의 회수율은 37.1%로서 정제도는 약 59배였으며 polyacrylamide gel electrophoresis에 의하여 단일 단백질띠를 보이는 순도를 나타냈다. Sephadex G-100 gel filtration에 의하여 측청된 분자의 크기는 약 47,000 dalton 이었고 p-chloromercuribenzene sulfonic acid 에 의해서 효소의 활성이 저해되었다. 효소의 최적 pH 는 8.0 정도였고 기질인 p-Nitrophenylacetate에 대한 반응은 Michaelis-Menten 이론에 부합되었으며 Km은 $166\;{\mu}M$ 이었다. 이 효소는 또한 p-nitrophenylpalmitate를 가수분해 하였으나 tripalmitin에는 거의 작용하지 않았다.
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송화가루로부터 p - Nitrophenylacetate Hydrolase 의 정제 및 효소의 특성
박진규,김유삼 ( Jin Kyu Park,Yu Sam Kim ) 생화학분자생물학회 1983 BMB Reports Vol.16 No.3
p-Nitrophenylacetate hydrolase was detected in the extracellular fluid of pine pollen and purified by the combination of DEAE cellulose ion exchange chromatography and Sephadex G-100 gel filtration. The purification steps resulted in about 59 fold purification with 37 % recovery of the enzyme activity. The purified enzyme showed a single protein band on the acrylamide gel after electrophoresis and the molecular weight of the enzyme was estimated to be 47,000 dalton by gel filtration with a calibrated Sephadex G-100 column. Its enzyme activity was inhibited by a thiol-directed reagent, p-chloromercuribenzene sulfonic acid. The optimum pH of this enzyme was 8.0 and a typical Michelis-Menten type saturation pattern with increasing concentration of p-nitrophenylacetate was obtained. From the double reciprocal plot its Km value was calculated to be 166 μM. This enzyme also hydrolyzed p-nitrophenylpalmitate but not tripalmitin.
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