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Copper–zinc superoxide dismutase from the marine yeast Debaryomyces hansenii
Author(s) -
HernándezSaavedra N. Y.,
Ochoa J. L.
Publication year - 1999
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(19990615)15:8<657::aid-yea410>3.0.co;2-u
Subject(s) - debaryomyces hansenii , superoxide dismutase , biology , biochemistry , enzyme , yeast , zinc , saccharomyces cerevisiae , dismutase , microbiology and biotechnology , trypsin , molecular mass , protein subunit , chemistry , gene , organic chemistry
We have isolated the cytosolic form of Cu–Zn superoxide dismutase (SOD) from the marine yeast Debaryomyces hansenii . This enzyme has a subunit mass of 18 kDa. The preparation was found to be heterogeneous by IF electrophoresis with two pI ranges: 5·14–4·0 and 1·6–1·8. The enzyme preparation had a remarkably strong stability at pH 6·0–7·0, surviving boiling for 10 min without losing more than 60% of activity. On Western blots, this enzyme was recognized by antibodies raised in rabbits against D. hansenii extracts, while only a weak cross‐reaction could be detected using antibodies generated against either Saccharomyces cerevisiae or bovine erythrocyte Cu–Zn SODs. In sequencing analysis, a peptide obtained by trypsin digestion was found to have 85% identity to the S. cerevisiae Cu–Zn SOD. Copyright © 1999 John Wiley & Sons, Ltd.