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유상하,홍광준,이상렬,신용진,이관교,서상석,김승욱,정준우,신영진,정태수,신현길,김택성,문종대,You S.H.,Hong K.J.,Lee S.Y.,Shin Y.J.,Lee K.K.,Suh S.S.,Kim S.U.,Jeong J.W.,Shin Y.J.,Jeong T.S.,Shin B.K.,Kim T.S.,Moon J.D. 한국결정학회 1997 韓國結晶學會誌 Vol.8 No.1
[ $CuInTe_2$ ] 다결정은 수평전기로에서 합성하고, $CuInTe_2$ 단결정은 수직 Bridgman 방법으로 성장시켰다. $CuInTe_2$ 단결정의 c축에 수직 및 평행한 시료의 광전도도와 광발광특성을 293K에서 20 K의 온도영역에서 측정하였다. 측정된 광전류 봉우리로부터 구한 c축에 수직 및 평행한 시료의 에너지 띠 간격은 상온에서 각각 0.948 eV와 0.952 eV였다. 광전류 봉우리와 광발광 봉우리의 에너지차는 포논에너지이며 상온에서 c축에 수직 및 평행한 시료의 에너지차는 각각 22.12 meV와 21.4 meV였다. 또한 광전류 스펙트럼으로부터 시료의 spin-orbit 상호작용과 결정장 상호작용에 의한 가전자대의 갈라짐 ${\Delta}cr$과 ${\Delta}so$는 각각 0.046, 0.014 eV였다. [ $CuInTe_2$ ] synthesised in a horizontal electric furnace was found to be polycrystalline. Single crystals of $CuInTe_2$ were grown with the vertical Bridgman technique. The photoconductivity and photoluminescence of the crystals were measured in the temperature range 20 to 293 K. From the photocurrent peaks measured for the samples both perpendicular and parallel to c-axis, the energy band gaps of the samples were found to be 0.948 eV and 0.952 eV at room temperature respectively. The energy difference of the photocurrent and photoluminescence peaks of the samples both perpendicular and parallel to the c-axis measured at room temperature was a phonon energy, and its values were 22.12 meV and 21.4 meV respectively. The splitting of the valence band due to spin-orbit and crystal field interaction was calculated from the photocurrent spectra of the samples, The ${\Delta}cr\;and\;{\Delta}so$ are 0.046,0.014 eV respectively.
박종래,김영주,이상렬 ( J . L . Park,Y . J . Kim,S . Y . Lee ) 한국축산학회 1974 한국축산학회지 Vol.16 No.3
Human milk sample was taken from 15 women living Sumon, Korea who are in the stage of 1 to 3 month after pasturition and its chemical composition, amino acids content and electrophoretical mobility were studied. The milk contained 2.36±0.66% of fat, 1.30±0.16% of protein, 7.25±0.34% of lactose and 0.12±0.03% of ash, and the ratio of casein to whey protein was 1 : 1.3. Human acid casein contained more amino acids such as Glu, Val, Ileu, and Leu but less amount of Ser, and Pro than that of Holstein milk. As human casein was analyzed for electrophoretic movibility, four main electrophoretic bands were formed at the position of bovine k-casein and no band was appeared at the position of bovine αs-casein when 6% polyacrylamide gel and tris-EDTA buffer pH 8.6 were used. Human whey protein did not appear at the position of bovine β-lactoglobulin while a large amount of lactoferrin was observed from the position of bovine immunoglobulin.