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Claviceps sp . 에서 Cytochrome P - 450 및 NADPH - Cytochrome c Reductase 정제 및 그 특성
김수언,김인수,John A . Anderson ( Soo Un Kim,In Soo Kim,John A . Anderson ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.3
Microsomes of Claviceps purpurea PRL 1980 had a maximum concentration of cytochrome P-450 of 40 pmole per ㎎ protein. Cytochrome P-450 and NADPH-cytochrome c reductase were purified from C. purpurea PRL 1980 microsomes to concentrations of 421 pmole per ㎎ protein and 387 pmole per min per mg protein, respectively. Activity was not reconstituted from these fractions, but NADPH-cytochrome c reductase increased agroclavine hydroxylase activity of C. purpurea PRL 1980 microsomes. The activity was not stimulated by rat liver microsomal NADPH-cytochrome c reductase. Claviceps sp. SD58 microsomal agroclavine hydroxylase had V_(max) of 3.3 pkat per ㎎ and K_m of 0.11 mM for agroclavine. Agroclavine bound to cytochrome P-450 from Claviceps sp. SD58 to give a type II spectrum. The absorbance maximum in the CO-reduced vs reduced difference spectrum of purified cytochrome P-450 from C. purpurea PRL 1980 and Claviceps sp. SD58 was at 449 ㎚.
김수언,김인수,Kim, Soo-Un,Kim, In-Soo,Anderson, John A. 생화학분자생물학회 1985 한국생화학회지 Vol.18 No.3
Claviceps, purpurea PRL 1980의 microsome에는 단백질 mg 당 40 pmole의 cytochrome P-450이 함유되어 있었다. 이 microsome으로부터 단백질 mg 당 420 pmole의 cytochrome P-450 및 387 pmole의 NADPH-cytochrome c reductase로 정제하였다. 부분 정제된 이 두 단백질로 재구성을 시도하였을 때 agroclavine hydroxylase 활성을 나타내지 않았으나 NADPH-cytochrome c reductase를 microsome에 첨가하였을 경우에는 그 활성이 80% 증가되었다. Claviceps sp. SD58의 microsome에 있는 agroclavine hydroxylase의 $V_{max}$와 $K_m$값은 agroclavine에 대하여 각각 3.3 pkat와 0.11 mM 이었다. 또 이 균으로부터 정제된 cytochrome P-450과 기질인 agroclavine의 복합체는 제2특성을 갖는 spectrum을 나타내었다. 또 위의 두 균주로 부터 분리한 cytochrome P-450이 이산화탄소와 결합할때 그 difference spectrum의 최대흡광은 449 nm 이었다. Microsomes of Claviceps purpurea PRL 1980 had a maximum concentration of cytochrome P-450 of 40 pmole per mg protein. Cytochrome P-450 and NADPH-cy-to chrome c reductase were purified from C. purpurea PRL 1980 microsomes to concentrations of 421 pmole per mg protein and 387 pmole per min per mg protein, respectively. Activity was not reconstituted from these fractions, but NADPH-cytochrome c reductase increased agroclavine hydroxylase activity of C. purpurea PRL 1980 microsomes. The activity was not stimulated by rat liver microsomal NADPH -cytochrome c reductase. Claviceps sp. SD58 microsomal agroclavine hydroxylase had $V_{max}$ of 3.3 pkat per mg and $K_m$ of 0.11 mM for agroclavine. Agroclavine bound to cytochrome P-450 from Claviceps sp. SD58 to give a type II spectrum. The absorbance maximum in the CO-reduced vs reduced difference spectrum of purified cytochrome P-450 from C. purpurea PRL 1980 and Claviceps sp. SD58 was at 449 nm.
Arteannuic acid 에서 epi - deoxyarteannuin B 의 효과적 합성
김수언 ( Soo Un Kim ) 한국응용생명화학회 1990 Applied Biological Chemistry (Appl Biol Chem) Vol.33 No.2
Oxidation of artemisinic acid was attempted with chromium trioxide-pyridine complex. Epi-Deoxyarteannuin B was formed almost quantitatively, while expected keto artemisinic acid was not the major product. The physical and spectral data. of the product are presented(Received March 9, 1990, Accepted May 25, 1990)
갈화 ( Puerariae flos ) 추출물이 Rat 혈중 Ethanol 농도에 미치는 영향
김정한(Jeong Han Kim),민선식(Sun Sik Min),김성훈(Sung Hoon Kim),홍희도(Heu Do Hong),김종수(Jong Soo Kim),김수언(Soo Un Kim) 한국응용생명화학회 1995 Applied Biological Chemistry (Appl Biol Chem) Vol.38 No.6
Ethanol concentration in blood, brain and liver of rats was shown to be effectively lowered by arrowroot flower extract. The lowering effect for ethanol concentration in blood was maximum when measured after 1 hour from ethanol feeding. Hot water extract was more effective than 80% ethanol extract. The treatment of extract at 10 min. before ethanol feeding gave a better result than that at 10 min after or 1 hour before ethanol feeding. The ethanol concentration in brain and liver was lowered as found in the blood ethanol concentration. Acetaldehyde was not detected either in blood or the tissues. The optimal amount of the Puerariae flos was 55.7㎎/㎏·body weight. The newly developed analytical method using dichloromethane as extracting solvent was proven to be very effective in terms of speed and simplicity.
녹두(Phaseolus aureus)와 팥(Phaseolus angularis)의 저장단백질의 분리와 그 특성에 관하여
이춘영,김수언,유기중,Lee, Chun-Yung,Kim, Soo-Un,Yoo, Ki-Jung 생화학분자생물학회 1978 한국생화학회지 Vol.11 No.3
녹두(P.aureus)와 팥(P.angularis)의 저장단백질을 Sephadex G-150으로 크로마토그라피하여 분리하고 그의 전기영동상 특성을 연구하였다. 분리된 단백질은 잠정적으로 Fl globulin 과 F2 globulin 으로 명명하였는데 각각 legumin과 vicilin으로 동정되었다. F2 globulin은 주 저장단백질로서 당단백질이었으며 disc-전기영동에서 확산된 하나의 분리대로 나타났다. 한편 SDS-전기영동과 PAW-전기영동에서는 작은 분리대 몇개가 주분리대와 함께 나타났다. SDS-전기영동에서 나타난 다섯 주분리대의 겉보기 분자량은 녹두에서 64,000, 53,000, 50,000, 27,000 그러고 23,400 이었으며 팥에서는 55,300, 53,000, 29,600, 26,600 그리고 25,000 이었다. A successful fractionation of the storage proteins in mung bean (P. aureus) and small red bean (P. angularis) seeds with chromatography on Sephadex G-150 was attained. Isolated proteins, tentatively designated as F2 globulin and F1 globulin, were classified as vicilin and presumably as legumin, respectively. Disc-PAGE of the major storage protein, F2 globulin, displayed a diffused band stained with periodic acid-Schiff's base reagent. However, SDS-PAGE demonstrated the faint bands besides five major bands. Apparent molecular weights of each subunit determined with SDS-PAGE were 64,000, 53,000, 50,000, 27,000 and 23,400 in F2 globulin of the mung bean and 55,300, 53,000 29,600, 26,600 and 25,000 in small red bean.
녹두 ( Phaseolus aureus ) 와 팥 ( Phaseolus angularis ) 의 저장단백질의 분리와 그 특성에 관하여
이춘영,김수언,유기중 ( Chun Yung Lee,Soo Un Kim,Ki Jung Yoo ) 생화학분자생물학회 1978 BMB Reports Vol.11 No.3
A successful fractionation of the storage proteins in mung bean (P. aureus) and small red bean (P. angularis) seeds with chromatography on Sephadex G-150 was attained. Isolated proteins, tentatively designated as F2 globulin and F1 globulin, were classified as vicilin and presumably as legumin, respectively. Disc-PAGE of the major storage protein, F2 globulin, displayed a diffused band stained with periodic acid-Schiff`s base reagent. However, SDS-PAGE demonstrated the faint bands besides five major bands:.Apparent molecular weights of each subunit determined with SDS-PAGE were 64,000 53,000. 50,000. 27,000 and 23,400 in F2 globulin of the mung bean and 55,300. 53,000 29,600 26,600 and 25,000 in small red bean.
색소 중간체와 개시체 투여가 Monascus 색소생산에 미치는 영향
홍영주(Young Ju Hong),김정구(Jeong Gu Kim),우현철(Hyun Chul Woo),김수언(Soo Un Kim) 한국응용생명화학회 1995 Applied Biological Chemistry (Appl Biol Chem) Vol.38 No.1
To investigate the mechanism for the main chain-elongation process and the possibility of putative precursors as stater units in the biosynthesis of the Monascus pigments, feeding experiments with possible poly-β-ketide intermediates were carried out. Both crotonic acid and sorbic acid. especially In low concentrations, enhanced the pigment production while not increasing the dried mycelium weight appreciably. Also, it was observed that the feeding of sorbic acid and its ethyl ester was about two folds efficient in the pigment production than the feeding of crotonic acid and its ethyl ester. In addition to these acids, cinnamic acid and vinylacrylic acid were examined for their possibility as starter units. It was observed that the color of the culture fed with cinnamic acid was dominantly dark-red, but with overall decrease in the pigment production. Whey its ethyl ester was administered to the culture. however, the pigment production increased significantly. Also noted in 2D TLC study o1 the pigments was the increased production of red pigment and the formation of new red pigments.