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P. Oyungerel,김홍진 한국몽골학회 2013 몽골학 Vol.0 No.35
This research aims to analyze the factors determining the export and import between Korea and Mongolia. Data were estimated and analyzed by quarter based time series through unit root tests and regression analysis. As a result, the model that the increase of income in both countries increase the import and the export between the two countries is convincing the most. The variables including the changes in relative prices and the change in exchange rate revealed weak explanatory power, except Mongolia's import equation. Therefore, in order to promote the trade, two countries need to endeavor to increase national income and the investment, and improve the productivity. Also, both countries need to aim at the improvement of competitiveness through the stabilization of macroeconomic variables, especially the stabilization of consumer prices. In Mongolia, the prices of the elements should be stabilized for the price stability.
이관호,P. K. Mandal,Hee-kyong Lim,Chi-Ho Lee,Oyungerel Baatartsogt,Gwang-Joo Jeon,Il-Shin Choe,최강덕 한국축산식품학회 2009 한국축산식품학회지 Vol.29 No.2
This study was conducted for the isolation, purification, and characterization of a protease from Korean pear, to see its proteolytic activity on chicken actomyosin and to find the optimum pH and temperature of activity on chicken actomyosin. The protease was isolated from crude extract of Korean pear by ammonium sulfate precipitation. Further purification was done by DEAE-Sepharose ion-exchange chromatography, Mono-Q and Mini-Q column chromatography. The purified enzyme gave a single protein band on SDS polyacrylamide gel electrophoresis and the molecular weight was found to be 38 kDa. The specific activity of purified enzyme was 34,907 unit/mg with 25 fold purification and the yield was 2%. The purified enzyme incubated with chicken actomyosin showed high activity. The optimum pH and temperature for enzyme activity on chicken actomyosin were 6.5 and 70℃, respectively. A protease was purified from Korean pear for the first time and characterized. It was found to be promising for meat tenderization
Guan, Hao-Li,Mandal, P.K.,Lim, Hee-Kyong,Baatartsogt, Oyungerel,Lee, Chi-Ho,Jeon, Gwang-Joo,Choe, Il-Shin,Choi, Kang-Duk Korean Society for Food Science of Animal Resource 2009 한국축산식품학회지 Vol.29 No.2
This study was conducted for the isolation, purification, and characterization of a protease from Korean pear, to see its proteolytic activity on chicken actomyosin and to find the optimum pH and temperature of activity on chicken actomyosin. The protease was isolated from crude extract of Korean pear by ammonium sulfate precipitation. Further purification was done by DEAE-Sepharose ion-exchange chromatography, Mono-Q and Mini-Q column chromatography. The purified enzyme gave a single protein band on SDS polyacrylamide gel electrophoresis and the molecular weight was found to be 38 kDa. The specific activity of purified enzyme was 34,907 unit/mg with 25 fold purification and the yield was 2%. The purified enzyme incubated with chicken actomyosin showed high activity. The optimum pH and temperature for enzyme activity on chicken actomyosin were 6.5 and $70^{\circ}C$, respectively. A protease was purified from Korean pear for the first time and characterized. It was found to be promising for meat tenderization.