http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : 류희문(Xi-Wen Liu) (검색결과 5 건)
- 무료
- 기관 내 무료
- 유료
-
권오윤(Oh-Yun Kwon),김미연(Mi Yeon Kim),손찬욱(Chan Wok Son),류희문(Xi-Wen Liu),김형진(Hyoung Chin Kim),윤원기(Won Kee Yoon),김환묵(Hwan Mook Kim),김미리(Mee Ree Kim) 한국식품영양과학회 2008 한국식품영양과학회지 Vol.37 No.1
국내에서 생산된 감자 중 세풍, 남서, 수미, 조풍 및 대서의 5가지 품종에 대하여 단백질 profile 및 아미노산 조성을 분석하였다. 총 질소함량은 1.27~1.64%이었으며, 남서가 높았고 수미가 낮게 나타났다. 아미노산 조성은 품종 간에 유의적인 차이가 있었다. 한편, 주요 감자 단백질은 papatin(40 kDa), trypsin inhibitor(20 kDa) 및 protease inhibitor(15 kDa)이었으며, 이들의 함량은 각각 22.16~25.81%, 25.22~20.91% 및 14.12~25.23%이었다. Papatin 함량은 조풍, 세풍, 수미감자가 높은 함량을 보인 반면, trypsin inhibitor는 조풍감자가 5.22%로 가장 낮은 함량을 보였다. Protease inhibitors인 20 kDa와 15 kDa를 합한 값은 24.7~35.0%이었으며, 세풍이 가장 적었고 조풍에 가장 많이 함유되어 있었다. The protein profiles of domestic potato cultivars were evaluated for total protein determination, amino acid composition, SDS-PAGE analysis and scanning densitometry. There were statistically significant differences in the levels of amino acids among potato cultivars. Total nitrogen amount was also significantly different among cultivars, ranging from 1.27 to 1.64%. SDS-PAGE analysis showed that there were significant differences in the content of major potato proteins such as papatin (40 kDa), trypsin inhibitor (20 kDa) and protease inhibitor (15 kDa) among cultivars (p<0.05). The amount of papatin among cultivars with a range of 22.16 to 25.81 mg/g d.w. was higher in Jopung, Shepody and Superior, whereas the amount of protease inhibitors including 15 kDa and 20 kDa was the highest in Jopung (37.0%). The Shepody contains the highest amount of papatin (25.8%) and the lowest of trypsin inhibitor (5.22%). Thus, it is suggested that Shepody is the most desirable cultivar for better nutrition based on the protein profile.
-
소 뇌 조직으로부터 5'-Nucleotidase의 정제 및 특성규명
류희문,석대은 충남대학교 약학대학 의약품개발연구소 2002 藥學論文集 Vol.17 No.-
5'-Nucleotidase, bound to brain membranes as a glycosylphosphatidyl-inositol (GPI)-anchored protein, is responsible for the conversion of adenosine-5'-monophosphate into adenosine, which is an agonist in adenosine receptor signalling. Here, 5'-nucleotidase was isolated from bovine brain using PI-PLC treatment, and purified by concanavalin A sepharose chromatography, DEAE-sephacel chromatography, and finally AMP affinity chromatography. For higher yield of enzyme purification, Zn^2+ was Included in the elution buffer in DEAE-sephacel chromatography. Especially, NaCl was more favorable than MgCl_2 for the elution of 5'-nucleotidase, proper for inactivation study, from AMP affinity column. The purified 5'-nucleotidase was relatively pure on SDS-PAGE analysis, showing a specific activity of 30.27 μmole/min/㎎ (purification fold 19,000 fold). The purified enzyme, possessing a K_m value of 44μM and an optimum pH of 7.5, was inhibited competitively by ATP (K_i, 12 μM), and uncompetitively by cysteine (K_i, 0.32 mM). In addition, the enzyme was activated slighty (1.5-folds) by Mg^2+.
-
효소 Lipoxygenase의 신규기질 : Acylglycerol, acylethanolamide, lysophospholipids 및 phospholipids
황룡쌍,류희문,박천호,석대은 충남대학교 약학대학 의약품개발연구소 2007 藥學論文集 Vol.22 No.-
Lipoxygenase belongs to a diverse family of nonheme ferroproteins that oxygenate polyenoic fatty acids containing 1,4-pentadiene structure to form their corresponding hydroperoxy derivatives. Lipoxygenases (LOXs), widely distributed in animals and plants, have a key function in the formation of biologically active substances from pulyunsaturated fatty acids. Generally, free polyunsaturated fatty acids, liberated from membrane phospholipids via phospholipase-catalyzed hydrolysis, are used as substrates for LOXs. Although it is acknowledged that free polyunsaturated fatty acids are preferred to phospholipids or triglycerides as substrates, there have been recent reports that mammalian enzymes can oxidize certain phospholipids. Especially, reticulocyte LOX (15-LOX) leukocyte 15-LOX, leukocyte LOX (12-LOX) can oxygenate complex substrates such as phospholipids and biomembranes. In addition, acylglycerol and acylethanolamide are utilized by lipoxygeanse as well as cycoloxygenase; the latter enzyme contributes to generation of bioactive prostanoids derivative. Furthermore, lysophosphatidylcholine or lysophosphatidic acid containing linoleoyl or arachidonoyl moieties are known to be oxygenated by reticulocyte LOX, leukocyte 15-LOX or leukocyte-type 12-LOX; oxygenated lysophospholipids can play a carrier role in transporting oxygenated derivatives. Thus, the use of various lipid substrates as new substrates for lipoxygenase may extend the physiological roles of those lipids containing unsaturated fatty acyl chains.
-
Cumene hydroperoxide에 의한 paraoxonase 1의 산화적 불활성화에 대한 보호 방안
스, 위엥쥐,류희문,김주령,석대은 충남대학교 약학대학 의약품개발연구소 2003 藥學論文集 Vol.18 No.-
Paraoxonase 1 (PON1), an enzyme associated with high density lipoprotein (HDL), is known to protect low density lipoprotein (LDL) from lipid peroxidation involving copper ion. However, Paraoxonase 1 activity was observed to decrease during LDL oxidation. Here, the inactivation of PON1 by various peroxides was examined. Paraoxonase 1, purified from human plasma, was subjected to cumene hydroperoxide, hydrogen peroxide or tert-butyl hydroperoxide. PON activity, based on the hydrolysis of phenyl acetate, decreased by approximately 40 and 38 %, respectively, after the exposure to 2mM cumene hydroperoxide and hydrogen peroxide, while tert-butyl hydroperoxide had no remarkable inhibitory effect. Next, the compounds capable of preventing against cumene hydroperoxide-induced inactivation of PONl were screened. While quercetin or phenyl acetate failed to protect PON1, lauric acid or calcium chloride was found to protect PONl from cumene hydroperoxide-induced inactivation. Especially, lauric acid appeared to show the greater protection than the other fatty acids tested. In further study, lauric acid showed a dose-dependent protection with an E& value of around 35 μM. Based on these results, It is proposed that the alky hydroperoxide-induced inactivation of Paraoxonase 1 can be prevented by a proper fatty acid recipe.
-
위엥쥐스,김주령,정태숙,류희문,석대은 충남대학교 약학대학 의약품개발연구소 2002 藥學論文集 Vol.17 No.-
Paraoxonase (PON), an enzyme associated with high density lipoprotein (HDL), is known to protect low density lipoprotein (LDL) from lipid peroxidation involving copper ion. However, PON activity was observed to decrease during LDL oxidation. Here, we attempted to elucidate the possible mechanism for the inactivation of PON. PON was partially purified from human plasma, and subjected to various oxidant systems. PON activity, based on the hydrolysis of phenyl acetate, decreased slightly after the exposure to H_2O_2 or ascorbate, while oxidants such as peroxynitrite or HOCl had no remarkable effect. Inclusion of Cu^2+ in the incubation with ascorbate (0.3∼1 mM) led to a rapid decrease of activity in a time-and concentration-dependent manner. In comparison, ascorbate/Cu^2+ system was much more effective than ascorbate/Fe^2+ system in inactivating PON. A further study indicates that general hydroxyl radical scavengers such as mannitol, ethanol or benzoate failed to prevent the PON inactivation. Based on these results, it is proposed that the PON inactivation during LDL oxidation may be ascribed mainly to the Cu^2+-catalyzed oxidation.
ScienceON
DBpia연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
