http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
김선진,정해승,Kim, Sun-Jin,Jeong, Hae-Seung 한국군사과학기술학회 2006 한국군사과학기술학회지 Vol.9 No.1
Experiments on film cooling were performed with a small scale rocket engine homing liquid oxygen (LOx) and Jet A-1(jet engine fuel). Film coolants(Jet A-1 and water) were injected through the film cooling injector. Film cooled length and the outside wall temperature of the combustor were determined for chamber pressure, and the different geometries(injection angle) with the flow rates of film coolant. The loss of characteristic velocity due to film cooling was determined for the case of film cooling with water and Jet A-1. As the coolant flow increases, the outside wall temperatures decrease but the decrease in the outside wall temperatures reduced over the 8 percent film coolant flow rate. The efficiency of characteristic velocity was decreased with the Increase of the film coolant flow rate.
소의 간 미토콘드리아 Matrix Aldehyde Dehydrogenase의 반응메카니즘에 관한 연구
김선진,주충노,Kim, Sun-Jin,Joo, Chung-No 생화학분자생물학회 1994 한국생화학회지 Vol.27 No.5
소의 간 mitochondria의 matrix에서 분리 정제한 aldehyde dehydrogenase(EC 1.2.1.3)의 초기반응속도와 NADH에 의한 반응억제 연구로부터 이 효소반응은 sequential mechanism이며 $NAD^+$가 효소에 먼저 결합한 후 aldehyde가 결합하고 생성물인 산이 먼저 이탈된 후 NADH가 이탈되는 ordered mechanism임을 알 수 있었다. 또한 이 효소는 dehydrogenase 활성 이외에 높은 esterase 활성을 나타내었다. Chloral hydrate에 의한 이 ALDH의 dehydrogenase 활성과 esterase 활성의 저해양상을 조사한 결과 $NAD^+$ 존재하에서는 dehydrogenase 활성을 경쟁적으로 저해하였지만 esterase 활성에 대해서는 mixed type의 저해양상을 나타내었다. Disulfiram의 억제반응에서 dehydrogenase의 반응 기질인 propionaldehyde는 disulfiram에 의한 dehydrogenase 활성저해를 보호하였지만 esterase 활성의 저해는 보호하지 못하였고 esterase의 반응기질인 p-nitrophenylacetate도 esterase의 활성저해를 보호하였지만 disulfiram에 의한 dehydrogenase 활성의 저해를 보호하지 못하였다. 또한 $100{\mu}M$ 이상의 $NAD^+$ 존재하에서는 esterase 반응이 $NAD^+$ 자체에 의해 저해되는 것으로 보아 dehydrogenase 반응과 esterase 반응이 반드시 같은 부위에서 일어난다고 생각하기는 어렵다. The initial velocity data and NADH inhibition behavior of the purified bovine liver mitochondrial matrix aldehyde dehydrogenase (EC 1.2.l.3, ALDH) indicated that the ALDH reaction might be proceeded by sequential ordered mechanism, first $NAD^+$ is bound with the enzyme followed by aldehyde and then the oxidized product (acid) would be removed followed by NADH This enzyme also showed esterase activity. We examined its esterase activity as well as dehydrogenase activity through various kinetic approchs and chemical modification techniques and we found that the active site of dehydrogenase reaction and esterase reaction might be different.
소의 간 미토콘드리아 Matrix Aldehyde Dehydrognease 의 정제 및 특성에 관한 연구
김선진,주충노 ( Sun Jin Kim,Chung No Joo ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.5
Bovine liver mitochodrial matrix aldehyde dehydrogenase (ALDH) was purified by ammonium sulfate precipitation, DEAF-Sephacel, hydroxyapatite and blue-Sepharose CL-6B column chromatography. The molecular weight of this enzyme was determined to be 230 KDa by S-300 gel filtration and it was realized that this enzyme was consisted of four identical subunits and molecular weight of its subunit was found to be 57.4 KDa by SDS-polyacrylamide gel electrophoresis, indicating that this enzyme is homotetramer. This ALDH was stable at 25∼37℃ and its optimum pH was 9.5. The K_m values of this enzyme for acetaldehyde and propionaldehyde were 9.6 μM and 6.5μM respectively but K_m values for biogenic aldehydes such as succinic semialdehyde and indole-3-acetaldehyde were relatively high (10^(-4) mM level), but not reactive with aromatic aldehydes, suggesting that this enzyme might participate mainly in the oxidation of short chain aliphatic aldehydes.
소의 간 미토콘드리아 Matrix Aldehyde Dehydrogenase 의 반응메카니즘에 관한 연구
김선진,주충노 ( Sun Jin Kim,Chung No Joo ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.5
The initial velocity data and NADH inhibition behavior of the purified bovine liver mitochondrial matrix aldehyde dehydrogenase (EC 1.2.1.3, ALDH) indicated that the ALDH reaction might be proceeded by sequential ordered mechanism, first NAD^+ is bound with the enzyme followed by aldehyde and then the oxidized product (acid) would be removed followed by NADH. This enzyme also showed esterase activity. We examined its esterase activity as well as dehydrogenase activity through various kinetic approchs and chemical modification techniques and we found that the active site of dehydrogenase reaction and esterase reaction might be different.
소의 간 미토콘드리아 Matrix Aldehyde Dehydrogenase의 정제 및 특성에 관한 연구
김선진,주충노,Kim, Sun-Jin,Joo, Chung-No 생화학분자생물학회 1994 한국생화학회지 Vol.27 No.5
소의 간 미토콘드리아의 matrix 분획으로부터 aldehyde dehydrogenase(EC 1.2.1.3, ALDH)를 황산암모늄 분별침전, DEAE-Sephacel, hydroxyapatite, blue-Sepharose CL-6B column chromatography로 정제하였다. S-300 gel filtration 방법으로 측정한 이 효소의 분자량은 230,000 dalton이고, 이 효소의 subunit을 SDS-polyacrylamide gel 전기이동법으로 조사한 결과 동일한 subunit(분자량 : 57,400 dalton)으로 구성된 homotetramer임을 알 수 있었다. 이 효소의 최적 pH는 9.5였고, $25{\sim}37^{\circ}C$에서 매우 안정하였다. Acetaldehyde와 propionaldehyde에 대한 $K_m$값은 각각 $9.6{\mu}M$, $6.5{\mu}M$이었으나 succinic semialdehyde나 indole-3-acetaldehyde에 대한 반응성은 매우 낮았고, 방향족 aldehyde에 대해서는 전혀 반응을 하지 않았다. 따라서 이 효소는 주로 short chain aliphatic aldehyde의 대사에 관여하는 것으로 생각된다. Bovine liver mitochodrial matrix aldehyde dehydrogenase (ALDH) was purified by ammonium sulfate precipitation, DEAE-Sephacel, hydroxyapatite and blue-Sepharose CL-6B column chromatography. The molecular weight of this enzyme was determined to be 230 KDa by S-300 gel filtration and it was realized that this enzyme was consisted of four identical subunits and molecular weight of its subunit was found to be 57.4 KDa by SDS-polyacrylamide gel electrophoresis, indicating that this enzyme is homotetramer. This ALDH was stable at $25{\sim}37^{\circ}C$ and its optimum pH was 9.5. The $K_m$ values of this enzyme for acetaldehyde and propionaldehyde were $9.6{\mu}M$ and $6.5{\mu}M$ respectively but $K_m$ values for biogenic aldehydes such as succinic semialdehyde and indole-3-acetaldehyde were relatively high ($10^{-4}$ mM level), but not reactive with aromatic aldehydes, suggesting that this enzyme might participate mainly in the oxidation of short chain aliphatic aldehydes.