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졸겔법으로 합성된 Mal<sub>2</sub>O<sub>4</sub>:Eu<sup>2+</sup>(M=Sr,Ba,Ca)의 특성
임규,김용현,이형직,김세기,이형복,Lim, Kyu,Kim, Young-Hyun,Lee, Hyung-Jik,Kim, Sei-Ki,Lee, Hyung-Bock 한국세라믹학회 2009 한국세라믹학회지 Vol.46 No.6
Phosphors of $Eu^{2+}$ doped alkaline earth aluminates MA$l_2O_4:Eu^{2+}$ (M=Sr, Ba, Ca) have been prepared by sol-gel process and their characterization of photoluminescence and photocurrent properties have been performed. The phosphors prepared by sol-gel process, due to its advantage of better homogeneity and low synthetic temperature, was synthesized as single phases at lower temperature than the solid-state process; $800{\sim}1000{^{\circ}C}$ for 6 h under mild reduction atmosphere (Ar- 3% $H_2$). It was confirmed that SrA$l_2O_4:Eu^{2+}$ composition revealed the most excellent properties in the brightness and photocurrent.
졸겔법으로 합성된 MAl2O4:Eu2+(M=Sr,Ba,Ca)의 특성
임규,김용현,김세기,이형복,이형직 한국세라믹학회 2009 한국세라믹학회지 Vol.46 No.6
Phosphors of Eu2+ doped alkaline earth aluminates MAl2O4:Eu2+ (M=Sr, Ba, Ca) have been prepared by sol-gel process and their characterization of photoluminescence and photocurrent properties have been performed. The phosphors prepared by sol-gel process, due to its advantage of better homogeneity and low synthetic temperature, was synthesized as single phases at lower temperature than the solid-state process; 800~1000 oC for 6 h under mild reduction atmosphere (Ar- 3% H2). It was confirmed that SrAl2O4:Eu2+ composition revealed the most excellent properties in the brightness and photocurrent.
임규인,류일선,Im, Gyu-In,Ryu, Il-Seon 한국낙농육우협회 2015 낙농·육우 Vol.35 No.12
젖소가 사료를 먹는 양은 생리학적으로는 혈당과 포만감에 의해 조절되며, 일반적으로 국내에서 사용하는 사료섭취량은 미국 NRC(국립과학연구소, The National Research Council)에서 실험 통계학적으로 나온 결과를 기준으로 품종, 산차, 체중, 비유시기, BCS(체점수), 기온 등을 고려하여 설정되었다. 최근 우리나라에서 풀의 사용량이 갈수록 증가하고 있는데 이에 따른 수익도 있지만 문제점은 없는지, 특히 생리학적인 면에서 한번은 짚고 넘어가야 한다고 보기 때문에 필자가 언급코자 한다.
임규리,홍윤표,노연이,김현정,김지영,( Gil-dong Hong ),( Cheol-soo Kim ),( Young-hee Lee ) 한국정보처리학회 2017 한국정보처리학회 학술대회논문집 Vol.24 No.2
다각도로 촬영할 수 있는 드론을 손동작으로 비행할 수 있고 드론이 자율비행을 하면서 동영상 및 사진을 촬영하여 드론에 장착된 플래시 메모리에 저장 및 근거리 무선통신으로 지상 방송국에 전송을 한다. ※카메라 연동 기술적 이슈로 인해, 참가 일정 내 카메라 부분 미완성 가능성 있음
林圭,洪承元,郭相太,黃炳斗 충남대학교 의과대학 지역사회의학연구소 1987 충남의대잡지 Vol.14 No.2
S-Adenosyl-L-methionine : protein-carboxyl 0-methyltransferase(prorein methylase II) has been purified from bovine skeletal muscle approximately 6,600-fold with a 7% yield by combination of ammonium sulfate precipitate, Sephadex G-75 chromatography, S-adenosyl-L-homocysteine-Sepharose 4B chromatography and hydroxyapatite chromatography, and then its characterizations and possible roles were investigated. The enzyme showed a optimum pH around 6.0. It was heat labile, inactivated by heat-treatment at 60℃ for 6 minutes, and when stored at -20℃ in the presence 10% glycerol, its activity has almost stabilized in 6 months. Copper ion(Cu^2+)and zinc ion(Zn^2+)were a potent inhibitors, the activity being completely inhibited at 0.25 mM and 1 mM respectively, The inhibition of copper and zinc ions were recovered 94%, 75% of its activity by adding 4 mM of EDTA, respectively. The apparent Km value for S-adenosyl--L-methionine was 2.86 x 10^-6 M. Kinetic analysis of enzyme in the presence of 30 uM copper ion showed that the nature of the inhibition to the enzyme was noncompetitive considering that Km was constant and Vmax was decreased. Histone IIA, immunoglobulin A and trypsin inhibitor were relatively good substrates for the enzyme. The enzyme activity was completely inhibited by 0.5 mM p-hydroxymercuribenzoic acid, but all of the activity was recovered in adding 10 mM mercaptoethanol, and the molecular weight of the enzyme was 24,000. Sarcolemma and sarcoplasmic reticulum of the skeletal muscle were good substrates for this enzyme and ^3H-CH_3 group was incorporated to 0.63 and 0.96 pmoles/mg protein/min, respectively. The carboxylmethylation of the sarcolemma of the skeletal muscle occurred in the 5 protein fractions(M. W. : 45,000, 22,000, below 14,400etc.) and that of sarcoplasmic reticulum occurred in the 7 protein fractions (M. W. : 100,000, 45,000, 22,000, below 14, 400 etc) by SDS/polyacrylamide gel electrophoresis. Among these molecular weight 22,000 was strongly methylated. These results discuss that protein methylase Il may play some roles in regulating physiological function of sarcolemma and sarcoplasmic reticulum of skeletal muscle.