The Power of Balance: Design that Conveys the philosophy and Culture of Samsung

한국의 삼성전자는 이제 글로벌 디자인 트렌드를 선도하는 트렌드세터로써 확고히 자리매김하고 있다. 삼성이 이런 디자인선도 브랜드로 거듭나게 된 배경에는,굿디자인이 브랜드의 가치와 이미지를 높인다는 디자인 경영전략이 있다. 삼성은 삼성만의 정신성을 담은 디자인 아이덴티티 프로그램 수립과 그에 기반한 디자인전력을 통하여 독자적인 브랜드이미지를 가진 디자인을 만들어 가고 있다. 이 아이덴티티 프로그램을 만들기 위하여 삼성은 모두가 공감할 수 있고, 한국의 문화를 대표할 수 있는 정체성을 찾는 데서 출발했고, 석굴암에 담겨진 지혜와 정신에서 삼성디자인이 추구해야 할 핵심가치를 찾아 내었다. 이 핵심가치는 인간중심: 사용자를 배려한 디자인으로 요약될 수 있으며 이 아이덴티티 프로그램을 근간으로 디자인 혁신 전략을 지속적으로 수행하여 글로벌 디자인 리더로서의 인정받고 있다

벼의 黑紫色 種皮가 品質 및 收量形質에 미치는 影響

학위논문(석사)--서울대학교 대학원 :농학과 작물학전공,2000.Maste

소 신장 Gamma-glutamyl transpeptidase 의 생리적 기능

학위논문(박사) - 한국과학기술원 : 생물공학과, 1990.8, [ xi, 121 p. ]Membrane bound $\gamma$ -GTP was purified from bovine kidne. The first purification method includes bromelain solublization acetone precipitation, salting out, DEAE-cellulose and Sehadex G-100 column chromatogtraphies. The purification folds and ield were 44.3 and 11.9\%, respectively. The second procedure includes microsome separation, Trition x-100 solublization, acetone treatment, gel filtration on Sephacryl S-300, and adsorption chromatography on hydroxyapetite column. The enzyme was purified by 393 folds and the yield was 18.6\%. The enzyme has a substrate specificity to $\gamma$ -glutamyl peptides and Sblocked $\gamma$ -glutamyl dipeptides were the best substrate among peptides tested. Dipeptides with glycine at its C-terminal end were bettter acceptros than other peptides. Among amino acids tested, methionine, cstein and glutamine can act as acceptors. Double reciprocal plots of the reaction velocities against varing the concentration of $\gamma$ -glutaml-p-nitroanilide at three fixed concentrations of glycylglycine showed parallel pattern. In vitro and in vivo $\gamma$ -GTP mediated amino acid transports were studied. Liposome incorporated with $\gamma$ -GTP didn``t transport methionine, alanine and leucine though methionine was a good acceptor among amino acids. In vivo experiments using unilaterial renal artery infusion also didn``t show any evidences that this enzyme participates in the amino acid translocation. The unilateral inection of $\gamma$ -GTP inhibitors (DON or Acivicine) or p-amino-hippurate induced a rise in pH of urine. The enzyme was activated by its own substrate in the absence of acceptor molecule but substrate activation disappeared in the presence of maleate or glyclglycine. At high concentrations of glcylglcine, product inhibition pattern was obsrved only in the presence of maleic acid. The $\gamma$ -GTP activity was inhibited competitively b maleate and the phenomena arised by was inhibited competitively by maleate and the phenome...한국과학기술원 : 생물공학과

Bovine skim milk sulfhydryl oxidase 의 부분정제, 특성 및 효소 반응 메카니즘에 관한 연구

학위논문 (석사) - 한국과학기술원 : 생물공학과, 1979.2, [ vii, 62 p. ]Sulfhydryl oxidase (EC 1.8.3.2) was purified partially by Sephadex G-100 and DEAE -cellulose column chromatography was purified about 1800 fold over the skim milk and showed optimum pH at 7.2 and optimum temperature at 37$^\circ$C. The activation energy of the enzyme was calculated to be 13.8 Kcal/mole by the Arrhenius equation. The molecular weight of the enzyme was verified to be 87,000 using Sephadex G-200 column chromatography. And it was confirmed that the enzyme acted on the conversion of sulfhydryl groups to their corresponding disulfides. This enzyme was inhibited by the addition of metal chelator, EDTA, but not by o-Phenanthroline,$\alpha,\alpha``$ -Dipyridyl which are iron specific chelators. And this enzyme requires $Mn^{++}$ for its activity. The application of functional group blocking agents and the photooxidation didn``t show the involvement of imidazole or hydroxyl groups in the active site of the enzyme. The enzyme obeyed Michaelis-Menten type kinetics at the low substrate concentrations but at the high substrate concentration above 0.83mM of GSH, substrate inhibition was observed. The Km and Vmax values were calculated to be $1.0\times10^{-4}$ M and 4.0 units per milligram protein, respectively. And this enzyme showed broad substrate specificity for thiol compounds bearing over two functional groups. Plots of 1/vo vs. 1/(cyst.) at various concentrations of fixed substrate $O_2$ showed uncompetitive type. And this enzyme was not inhibited by a product, disulfides, under saturated $O_2$ concentration. These results represent that the complex of enzyme-substrate, from which disulfides depart, leaving hydrogenated enzyme. Oxygen then combines with the hydrogenated enzyme to give the complex of two, which decomposes to yield the product $H_2O_2$ and free enzyme.한국과학기술원 : 생물공학과