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진주 담치로부터의 Superoxide Dismutase 의 정제와 특성
김세권,박선주,최광덕 ( Se Kwon Kim,Sun Joo Park,Kwang Duck Choi ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.5
Superoxide dismutase (SOD) was isolated by direct extraction method from the muscular tissue of Mytilus edulis. The enzyme was purified 264-fold with 1% yield for the cytosolic SOD by (NH₄)₂SO₄ fractionation, DEAF-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel chromatography. The molecular weight of the enzyme estimated from gel filtration on Sephadex G-100 was approximately 105.4 kDa and SDS-polyacrylamide gel electrophoresis also showed that it was composed of two identical subunits whose molecular weight was 52.9 kDa. The purified enzyme stably remained between pH 6 and pH 8.3 at 25℃, but was rapidly inactivated above pH 10.5 and below pH 5.0. This enzyme was easily inhibited by CN^-, Cl^-, H₂O₂, EDTA and SDS but was little inhibited by N₃^-. The absorption spectrum showed maximum peaks at 520 nm and 265 nm, but peak at 265 nm disappeared when treated with trace of cysteine. And atomic absorption spectroscopy indicated approximately 2 atoms of Cu^(2+) and Zn^(2+) per mol enzyme. Thus, the result on this special properties showed that SOD was composed of Cu/Zn-form.
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진주 담치로부터의 Superoxide Dismutase의 정제와 특성
김세권,박선주,최광덕,Kim, Se-Kwon,Park, Sun-Joo,Choi, Kwang-Duck 생화학분자생물학회 1994 한국생화학회지 Vol.27 No.5
풍부한 해양생물인 진주담치의 조직으로부터 분리정제된 superoxide dismutase(SOD)는 1%의 수율로 264배 정제되었다. 황산암모늄 처리, DEAE-Sephadex A-50 이온교환 크로마토그래피, Sephadex G-100 겔크로마토그래피를 이용해 정제된 효소는 Sephadex G-100 겔여과 방법으로 측정된 분자량이 105.4 kDa이었으며, SDS-polyacrylamide 전기이동을 행한 결과 52.9 kDa의 2개의 subunit로 구성된 homodimer 임이 밝혀졌다. 이 효소는 $25^{\circ}C$에서 완충용액의 pH가 6에서 8.3사이일 때는 매우 안정하였지만 pH5.0 이하나 pH 10.5 이상에서는 활성이 급격히 저해되었고, $CN^-$, $Cl^-$, $H_{2}O_{2}$, EDTA, SDS 농도에 비례하여서 활성이 억제되었다. 그러나 $N_{3}^{-}$는 효소활성에 영향을 주지 못하였다. 그리고 520nm와 265nm에서 최대의 흡광을 나타내었으며, 265nm에서의 흡광은 cysteine에 의해 쉽게 환원되었다. 또한 원자흡광분석기에 의해 측정된 결과, 효소몰당 2atom씩의 $Cu^{2+}$, $Zn^{2+}$가 각각 포함되어 있어 진주담치로부터 분리된 이 효소가 Cu/Zn-SOD임을 확인하였다. Superoxide dismutase (SOD) was isolated by direct extraction method from the muscular tissue of Mytilus edulis. The enzyme was purified 264-fold with 1 % yield for the cytosolic SOD by $(NH_{4})_{2}SO_{4}$ fractionation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel chromatography. The molecular weight of the enzyme estimated from gel filtration on Sephadex G-100 was approximately 105.4 kDa and SDS-polyacrylamide gel electrophoresis also showed that it was composed of two identical subunits whose molecular weight was 52.9 kDa. The purified enzyme stably remained between pH 6 and pH 8.3 at $25^{\circ}C$, but was rapidly inactivated above pH 10.5 and below pH 5.0. This enzyme was easily inhibited by $CN^-$, $Cl^-$, $H_{2}O_{2}$, EDTA and SDS but was little inhibited by $N_{3}^{-}$. The absorption spectrum showed maximum peaks at 520 nm and 265 nm, but peak at 265 nm disappeared when treated with trace of cysteine. And atomic absorption spectroscopy indicated approximately 2 atoms of $Cu^{2+}$, $Zn^{2+}$ per mol enzyme. Thus, the result on this special properties showed that SOD was composed of Cu/Zn-form.
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이응호,이원희,김세권,변희국,최광덕,노호석 한국수산학회 1993 한국수산과학회지 Vol.26 No.2
Collagenase existed in the internal organs of filefish Novoden modestrus was isolated with ammonium sulfate and was purified by ion exchange column chromatography with DEAE-Sephadex A-50 and gel filtration with Sephadex G-150. The activity of the purified enzyme was increased 92.4 folds than that of the crude one and the yield of the purified one was 10.9%. The optimum conditions showing the maximum activity of the crude enzyme to digest insoluble collagen(Type I) were 55℃ and pH 8.0, while those showing the maximum activity of the purified one were 55℃ and pH 7.75. However, the use of the crude enzyme for skinning of filefish was more profitable because the yield was 800 folds higher than that of the purified one and the cost was also able to economy. When hydrolysis for skinning of filefish was conducted with 0.3%(w/w) crude collagenase at 50℃ and pH 8.0 for 3hrs, there was some problem to cause a damage on muscle of the fish by heat. To solve such problem for the skinning, the hydrolysis at 18℃ for 4hrs with 0.3%(w/w) crude enzyme after pretreated with 0.5M acetic acid for 10 min provided a good result for skinning of filefish.
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