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쥐의 뇌 시토졸 Aldehyde Dehydrogenase의 정제 및 특성에 관한 연구
이향숙,주충노,Lee, Hyang-Sook,Joo, Chung-No 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.6
쥐의 뇌 시토졸 분획으로부터 aldehyde dehydrogenase(ALDH. EC 1.2.1.3)를 황산암모늄 분별침전, DEAE-Sephacel, Blue Sepharose CL-6B, 5'-AMP Sepharose 4B affinity chromatography 방법으로 분리 정제하였다. Short chain aliphatic aldehyde나 aromatic aldehyde에 대한 $K_m$값은 $10^{-3}M$ 수준이 었고 indole-3-acetaldehyde에 대 한 $K_m$값은 $10^{-4}M$ 수준이었으나, succinic semialdehyde에 대해서는 매우 낮은 $K_m$값($10^{-6}M$ 수준)을 나타내었으며 친화력도 가장 큰 것으로 보아 ${\gamma}-aminobutyrate$ 대사와 연관성이 큰 것으로 생각된다. $NAD^+$에 대한 $K_m$값($10^{-5}M$ 수준)은 $NADP^+$에 대한 $K_m$값($10^{-4}M$ 수준)의 1/10 정도이였으며 $NAD^+$가 주로 보조효소로 작용하는 것으로 생각된다. 이 효소의 disulfiram에 의한 억제현상은 disulfiram의 농도가 $10{\mu}M$일 때 효소활성이 약 15% 감소되었으나, disulfiram의 농도가 $25{\mu}M$로 증가하여도 약 30%의 효소활성은 남아있었다. 또한 이 효소는 dehydrogenase 활성외에 esterase 활성을 나타내었고 iodoacetamide, phenylmethylsulfonylfluoride, pyridoxal-5'-phosphate 등에 의해 활성 이 억제 되는 것으로 보아 cysteine, serine, lysine같은 아미노산 잔기가 효소활성 부위에서 중요한 역할을 할 것으로 생각된다. Rat brain cytosolic aldehyde dehydrogenase (ALDH, EC 1.2.1.3) was purified by ammonium sulfate precipitation, DEAF-Sephacel, Blue Sepharose CL-6B and 5'-AMP Sepharose 4B affinity chromatography. $K_m$ values of the cytosolic ALDH for short chain aliphatic aldehyde and aromatic aldehyde were $10^{-3}M$ level and that for indole-3-acetaldehyde was $10^{-4}M$ level. However, this enzyme had a very low $K_m$ value ($10^{-6}$ level) and the greatest affinity for succinic semialdehyde suggesting that the cytosolic ALDH seemed to be closely related to the metabolism of ${\gamma}-aminobutyrate$. $K_m$ of this enzyme for NAD was $10^{-5}M$ level while that for $NADP^+$ was $10^{-4}M$ level. It seemed that $NAD^+$ might be mainly used as a cofactor of this enzyme. Rat brain cytosolic ALDH was sensitive to disulfiram and the enzyme activity decreased to about 50% in the presence of $10{\mu}M$ disulfiram but 30% of the total activity of this enzyme remained even in the presence of $25{\mu}M$ disulfiram. This enzyme had esterase activity as well. It was realized that iodoacetamide, phenylmethylsulfonylfluoride, pyridoxal-5'-phosphate inhibited the enzyme activity suggesting that amino acid residues such as cys-teine, serine, lysine might participate at the active site of this enzyme.
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쥐의 뇌 시토졸 Aldehyde Dehydrogenase 의 정제 및 특성에 관한 연구
이향숙,주충노 ( Hyang Sook Lee,Chung No Joo ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.6
Rat brain cytosolic aldehyde dehydrogenase (ALDH, EC 1.2.1.3) was purified by ammonium sulfate precipitation, DEAF-Sephacel, Blue Sepharose CL-6B and 5`-AMP Sepharose 4B affinity chromatography. K_m values of the cytosolic ALDH for short chain aliphatic aldehyde and aromatic aldehyde were 10^(-3)M level and that for indole-3-acetaldehyde was 10^(-4)M level. However, this enzyme had a very low Km value (10^(-6) level) and the greatest affinity for succinic semialdehyde suggesting that the cytosolic ALDH seemed to be closely related to the metabolism of γ-aminobutyrate. K_m of this enzyme for NAD was 10^(-5)M level while that for NADP+ was 10^(-4) M level. It seemed that NAD+ might be mainly used as a cofactor of this enzyme. Rat brain cytosolic ALDH was sensitive to disulfiram and the enzyme activity decreased to about 50% in the presence of 10 μM disulfiram but 30% of the total activity of this enzyme remained even in the presence of 25 μM disulfiram. This enzyme had esterase activity as well. It was realized that iodoacetamide, phenylmethylsulfonylfluoride, pyridoxal-5`-phosphate inhibited the enzyme activity suggesting that amino acid residues such as cys-teine, serine, lysine might participate at the active site of this enzyme.
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