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Trehalase 에 관한 연구 (I) Sarcoma 180 복수암에 걸린 Mouse Trehalase에 관하여
권종만,이희성,이근배,Kwon, Jong-Man,Lee, Hi-Sung,Lee, Keun-Bai 생화학분자생물학회 1980 한국생화학회지 Vol.13 No.2
Mouse에 이식한 Sarcoma 180 복수암세포 및 복수에서 trehalase ($\alpha$, $\alpha-$ trehalose 1-D-glucohydrolase, EC 3. 2. 1. 28)의 분포를 관찰하였으며 이 효소를 부분 정제하였다. Trehalase의 활성도는 Lapp and Mason 법으로 측정하였으며 효소의 정제는 ammonium sulfate에 의한 침전 DEAE-cellulose column chromatography 및 Sephadex G-200 chromatography 등을 행하여 다음과 같은 결혼을 얻었다. 1. Sarcoma 180 복수암세포는 trehalase가 함유되어 있지 않다. 2. 7일만에 채취한 복수에서 이 효소의 활성도는 938.54 unit/ml이었다. 3. 복수의 이 효소의 활성도는 곤충, 기생충 및 미생물에 비하여 매우 낮았다. 4. 복수의 이 효소를 약 58배 정제하였으며 비활성도는 414.5이었다. 5. 이 효소의 반응 최적온도는 $60^{\circ}C$이며 반응최적 pH는 5.4 이다. 6. 이 효소는 glucose를 함유한 disaccharide의 기질중 trehalose에만 반응성이 있다. 7. 반응 생성물이 glucose임을 paper chromatography로 확인할 수 있었다. 8. 이상과 같은 결과로 보아 Sarcoma 180 복수암세포를 함유한 마우스의 복수에 trehalase가 존재함을 알 수 있었다. The activity of trehalase ($\alpha$, $\alpha-$ trehalose 1-D-glucohydrolase, ED 3. 2. 1. 28) in Sarcoma 180 ascites tumor cells and ascitic fluid which harvested at 7 days after transplantation has been studied. The activity of trehalase was measured by the method of Lapp and Mason. The results obtained were as follows; 1. The activity of trehalase could not be found in the Sarcoma 180 ascites tumor cells. 2. The activity of trehalase in ascitic fluid was 938.54 unit/ml. 3. In the ascitic fluid, the trehalase activity is relatively low compared with those in insect. microorganism, Ascaris suum and mouse kidney. 4. Trehalase from ascitic fluid has been purified about 58 fold by ammonium sulfate precipitation, DEAE-cellulose column chromatography and Sephadex G-200 gel filtration. 5. The optimal pH for enzymatic activity was 5.4, and optimal temperature was $60^{\circ}C$. 6. The enzyme was specific for trehalose as substrate. 7. The product of the reaction was identified as glucose by paper chromatographic method.
Trehalase 에 관한 연구 ( 1 ) Sarcoma 180 복수암에 걸린 Mouse Trehalase 에 관하여
권종만,이희성,이근배 ( Jong Man Kwon,Hi Sung Lee,Keun Bai Lee ) 생화학분자생물학회 1980 BMB Reports Vol.13 No.2
The activity of trehalase (α, α-trehalose 1-D-glucohydrolase, ED 3. 2. 1. 28) in Sarcoma 180 ascites tumor cells and ascitic fluid which harvested at 7 days after transplantation has been studied. The activity of trehalase was measured by the method of Lapp and Mason. The results obtained were as follows; 1. The activity of trehalase could not be found in the Sarcoma 180 ascites tumor cells. 2. The activity of trehalase in ascitic fluid was 938.54 units/㎖. 3. In the ascitic fluid, the trehalase activity is relatively low compared with those in insect, microorganism, Ascaris suum and mouse kidney. 4. Trehalase from ascitic fluid has been purified about 58 fold by ammonium sulfate precipitation, DEAE-cellulose column chromatography and Sephadex G-200 gel filtration. 5. The optimal pH for enzymatic activity was 5.4, and optimal temperature was 60℃. 6. The enzyme was specific for trehalose as substrate. 7. The product of the reaction was identified as glucose by paper chromatographic method.
권종만(Jong-Man Kwon),권철휘(Chul-Hui Kwoun),박성현(Sung-Hyun Park) 한국정보기술학회 2012 한국정보기술학회논문지 Vol.10 No.9
This paper proposes a basic research about development of an automatic observation system for low altitude surface temperature monitoring in coastal areas. The observation equipment is designed to capture the images from infrared thermal camera and measure the surface water temperature in the sky with 100m height using flying a balloon. The captured images at the observation equipment are sent to a server via Wi-Fi communication with the 5.8 GHz protocol and processed to monitor and analyze the surface water temperature by server program. The proposed system is capable of remote monitoring around a fixed place providing an accurate surface water temperature by analysis results. This system reduces the financial damages by a real time monitoring supporting useful information to people such as the management of fishery and cultivation, and a red and green tide effects.
사람태반 미토콘드리아의 Superoxide Dismutase의 정제 및 성상
권종만,이동욱,이희성 중앙대학교 의과대학 의과학연구소 1983 中央醫大誌 Vol.8 No.1
Cytotoxic superoxide radical(O_2^-) is a common intermediate of oxygen reduction reaction in the respiring cells and therefore these cells should be protected against the cytotoxic effect of superoxide radicals. At the present time, three types of superoxide dismutase, copper- and zinc-containing, iron-containing and manganese- containing superoxide dismutase, have been isolated from both eukaryotic and prokaryotic cells. The purification and properties of cytosolic superoxide dismutase of human term placenta have been reported previously from this laboratory. In this study, therefore, the experiment was carried out to characterize mitochondrial .superoxide dismutase of the placenta. Mitochondria of human placenta were isolated from human term placenta cell homogenate by differential centrifugation and the mitochondrial superoxide dismutase was purified by DEAE-cellulose column chromatography. The results were summarized as follows: 1. The distribution of superxode dismutase in terms of activity, in the cytosolic and mitochondrial fractions was found being 85%(7.4 units/g) and (1.3 units/g) respectively. 2. The distribution of mitochondrial superoxide dismutase in intermembrane space and matrix of mitochondria was found being 47% and 53% respectivly. 3. The mitochondrial superoxide dismutase was purified approximately 52 fold. The molecular weight of the purified enzyme was estimated to be 85,000 by Sephadex G-100 gel filtration method. 4. Purified mitochondrial superoxide dismutase contained 1.82 atoms of manganese per molecule and was very similar to the superoxide dismutase previously isolated from other eukaryotes. 5. The activity of manganese-containing superoxide dismutase was inhibited about 10% by 1mM cyanide but it is inhibited as much as 88% by ethanol-chloroform(5:1, v/v) mixture. 6. The ultraviolet absorption spectrum of purified mitochondrial superoxide dismutase was also similar to those of the previously prepared eukaryotic enzyme. 7. The activity of xanthine oxidase of human term placenta was found to be 23.6 units/g and the relative activity in the cytosolic and mitochondrial xanthine oxidase was 83% and 17%, respectively.