소의 간 미토콘드리아 Matrix Aldehyde Dehydrognease 의 정제 및 특성에 관한 연구 = Purification and Characterization of Bovine Liver Mitochondrial Matrix Aldehyde Dehydrogenase

다국어 초록 (Multilingual Abstract)

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.