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 : 주충노 ( Hyon Seo Koo (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
-
Aldehyde Dehydrogenase의 반응 메카니즘에 관한 연구 -Dehydrogenase 활성의 속도결정 단계의 추구-
주충노,김두식,구현서,김주휘,Joo, Chung-No,Kim, Doo-Shik,Koo, Hyon-Seo,Kim, Joo-Hwee 생화학분자생물학회 1992 한국생화학회지 Vol.25 No.6
소의 간 aldehyde dehydrogenase(ALDH)와 사람 적혈구 ALDH에 미치는 금속이온의 영향과 화학변형 실험을 행하고 보고된 ALDH의 반응 메카니즘에 관한 실험결과들을 종합하여 광범위한 특이성을 가진 일반 ALDH의 dehydrogenase 활성의 속도제한 단계가 Enzyme-NADH complex로부터의 NADH의 해리단계임을 알 수 있었다. The effect of several ions and chemical modification experiments using bovine liver cytosolic aldehyde dehydrogenase (ALDH) and human erythrocyte ALDH have been carried out to understand the rate-limiting process of dehydrogenase activity. From the previously reported experimental results and this study suggested that the releasing step of NADH from Enzyme-NADH complex might be a rate-limiting process.
-
Aldehyde Dehydrogenase 의 반응 메카니즘에 관한 연구 - Dehydrogenase 활성의 속도결정 단계의 추구
주충노,김두식,구현서,김주희 ( Chung No Joo,Doo Shik Kim,Hyon Seo Koo,Joo Hwee Kim ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.6
The effect of several ions and chemical modification experiments using bovine liver cytosolic aldehyde dehydrogenase (ALDH) and human erythrocyte ALDH have been carried out to understand the rate-limiting process of dehydrogenase activity. From the previously reported experimental results and this study suggested that the releasing step of NADH from Enzyme-NADH complex might be a rate-limiting process.
-
쥐간 미토콘드리아의 외막결합 Aldehyde Dehydrogenase 의 활성부위에 관한 연구
구현서,주충노 ( Hyon Seo Koo,Chung No Joo ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.5
The outer membrane bound ALDH of rat mitochondria was purified and its reaction phenomena were investigated through chemical modifications. The purified membrane bound ALDH was inhibited up to about 50% by disulfiram when its concentration was high and it was realized that at 0.1∼0.4 mM of sulhydryl specific iodoacetamide concentration, the ALDH was inhibited by the formation of enzyme inhibitor complex in one to one ratio of molecular level. The second-order rate constant was 334.3 M^-1min^-1. The purified outer membrane bound ALDH was also rapidly inactivated by thiol specific reagent such as phydroxymercuribenzoate at the concentration of 0.2∼0.6 μM. Inactivation by p-hydroxymercuribenzoate was protected by acetaldehyde, a substrate of ALDH. The second-order rate constant for the inactivation was calculated to be 773,000 M^-1min^-1, and the reaction order with respect to p-hydroxymercuribenzoate was 1.08, indicating that there might be one sulfhydryl residue per enzyme. Arginine specific reagent such as phenylglyoxal, histidine specific reagent such as diethylpyrocarbonate and lysine specific reagent such as pyridoxal 5`-phosphate have no effect on the above ALDH. However, phenylmethylsulfonyl fluoride, a serine specific reagent, inactivated ALDH as much as 66%. These results indicated that the cysteine, serine residues might probably be located at/or near the active site of the enzyme.
-
소의 간 시토졸 알데히드 탈수소효소의 정제와 특성에 관한 연구
구현서,주충노 ( Hyon Seo Koo,Chung No Joo ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.5
Cytosolic aldehyde dehydrogenase (ALDH) of bovine liver was purified by ammonium sulfate precipitation, DEAE-Sephacel column chromatography, hydroxyapatite affinity chromatography and 5`-AMP Sepharose 4B affinity chromatography. The molecular weight of cytosolic ALDH was determined to be 205,000 dalton by Sephadex G-150 gel filtration. SDS-polyacrylamide gel electrophoresis showed that it was homotetramer of four identical subunits, molecular weight of each of which was 52,000 dalton. Optimal pH and optimal temperature of this enzyme was found to be pH 9.0 and 37℃ respectively. The isoelectric point of this enzyme was 6.3. K_m values of bovine liver cytosolic ALDH for acetaldehyde, propionaldehyde, succinic semialdehyde was high (4∼6 mM) but those for benzaldehyde and indole 3-acetaldehyde were extremely low (20∼50 μM). This result suggested that bovine liver cytosolic ALDH might contribute partly to acetaldehyde oxidation in ethanol metabolism but its major function would be to oxidize biogenic aldehydes. It was realized that the esterase activity of bovine liver cytosolic ALDH was inhibited by propionaldehyde, a substrate of the dehydrogenase activity of this enzyme, suggesting that the catalytic site of dehydrogenase and esterase activity might be identical. Chloral hydrate protected N-ethylmaleimide inhibition of both dehydrogenase and esterase activity of this enzyme. This again suggested that both active sites might be identical. v
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
