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쥐의 간 미크로좀 Aldehyde Dehydrogenase 의 기능
조은위,주충노 ( Eun Wee Cho,Chung No Joo ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.4
One of the rat liver microsomal ALDH isozymes was purified and characterized and its probable physiological function was discussed. This microsomal ALDH was identified to be a tetramer consisting of 4 identical subunits, molecular weight of which was determined to be 55,000 daltons by SDS-gel electrophoresis. The molecular weight of the native ALDH was found to be 234,00 daltons by gradient gel electrophoresis. Both NAD^+ and NADP^+ could be used as cofactors for ALDH but its afffinity for NAD^+ was much greater than for the latter. The activity of ALDH increased sharply with increasing pH up to pH 10. 100 μM Hg^(+2) and/or 100 μM Ag^(+2) completely inhibited ALDH activity. Disulfiram inactivated ALDH activity. K_m for aliphatic aldehydes, either saturated or unsaturated of C₃C_9, decreased with increasing carbon chain length. Affinity of the enzyme for saturated aldehyde was greater than for unsaturated aldehydes from the data of their V_(max)/K_m. However the enzyme affinity for indole-3-acetaldehyde formed from indolamine was much smaller than for aliphatic aldehydes. These results suggest that the microsomal ALDH may play an important role in the oxidation of fatty aldehydes produced during lipid peroxidation of microsomal membranes. In connection to ethanol metabolism, lipid peroxide accumulation in the liver, increase of the acetaldehyde concentration in blood and liver, low NAD^+/NADH ratio and ALDH activity in the liver of ethanol administered rats suggest that acetaldehyde originated from ethanol administration and aldehydes formed during lipid peroxidation might compete for the microsomal ALDH resulting in the delay of both acetaldehyde and fatty aldehyde metabolism.
Tertiary Structure of PreS1(21-47) of Hepatitis B Virus Studied by NMR Spectroscopy
유경희,조은위,신송엽,김길룡,김양미 한국자기공명학회 2000 Journal of the Korean Magnetic Resonance Society Vol.4 No.1
To design more efficient peptide antagonist against the HBV, preS1(21-47) which carries the HBV receptor binding site for hepatocytes was synthesized and the solution structure of preS1(21-47) was investigated using CD spectroscopy and NMR spectroscopy in membrane-mimicking environments. According to CD spectra, preS1(21-47) has a random structure in aqueous solution, while conformational change was induced by addition of TFE and SDS micelle. Tertiary structure as determined by NMR spectroscopy shows that preS1(21-47) has a very flexible structure even in SDS micelle. 영어논문