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Catalases protect cellular proteins from oxidative modification in Saccharomyces cerevisiae
Author(s) -
Lushchak Volodymyr I.,
Gospodaryov Dmytro V.
Publication year - 2005
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2004.11.001
Subject(s) - catalase , biochemistry , dehydrogenase , yeast , oxidative phosphorylation , glucose 6 phosphate dehydrogenase , saccharomyces cerevisiae , chemistry , peroxisome , enzyme , antioxidant , cytosol , ethanol , gene
The yeast Saccharomyces cerevisiae cells had higher antioxidant enzyme activities under growth in ethanol than that in glucose as a carbon and energy source. The correlations between catalase activity and protein carbonyl level ( r 2 = 0.857), between catalase and glucose‐6‐phosphate dehydrogenase activities ( r 2 = 0.924) and between protein carbonyl levels and glucose‐6‐phosphate dehydrogenase activity ( r 2 = 0.988) under growth in ethanol were found. Growing in ethanol the strain deficient in cytosolic and peroxisomal catalases had 7.1‐fold higher level of carbonyl proteins than that of wild‐type strain. Our data suggest that in vivo catalases may protect glucose‐6‐phosphate dehydrogenase against oxidative inactivation.