Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 0613820090190091321
Journal of Life Science
2009 Volume.19 No. 9 p.1321 ~ p.1327
Effects of Amino Acids on the Activities of Alcohol Metabolizing Enzyme Alcohol Dehydrogenase (ADH) and Acetaldehyde Dehydrogenase (ALDH)
Cha Jae-Young

Jung Hae-Jung
Jung Jae-Jun
Yang Hyun-Ju
Kim Yong-Taek
Lee Yong-Soo
Abstract
The present study examined the comparative effects of various amino acids on the alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) activities of yeast Saccharomyces cereviciae and rat liver homogenate in vitro. Methionine showed the highest activity in yeast ADH among the amino acids used in this study, but this was not higher than that of the hangover product, Condition-Power (CP) used as positive control. Methionine was also found to be the best amino acid in terms of the ALDH activity in rat liver homogenate among the treatment amino acids, which was comparatively higher than that of positive control CP. It was chosen for further experiments and yeast ADH activity increased in parallel with increased methionine concentration, but not rat liver ALDH activity, and it was comparatively higher than those of the positive control. Arginine showed the highest values in yeast ALDH and rat liver ADH activities among amino acids, and it was chosen for further experiments. Yeast ALDH activity increased in parallel with increased arginine concentration, which was higher than that of positive control CP, and rat liver ADH activity was also comparatively higher in all treatment concentrations of arginine than that of positive control CP. The native electrophoresis of ADH and ALDH from cell-free extracts of yeast Saccharomyces cerevisiae cultured in the growth medium containing various arginine concentrations by 0¢¦0.1% showed two active bands upon zymogram staining analysis, and the straining intensity of ADH and ALDH active bands in arginine treatment yeast was stronger than that of non-yeast or low treatment yeast. These results indicate that alcohol metabolizing enzyme activities can be enhanced by arginine and methionine, suggesting that arginine and methionine have potent ethanol-metabolizing activities.
KEYWORD
Alcohol dehydrogenase(ADH), acetaldehyde dehydrogenase(ALDH), amino acid, arginine, methionine
FullTexts / Linksout information
Listed journal information
ÇмúÁøÈïÀç´Ü(KCI)