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Purification of isocitrate lyase from Saccharomyces cerevisiae
Author(s) -
LopezBoado Yolanda S.,
Herrero Pilar,
Fernandez MariaTeresa,
Fernandez Rose,
Moreno Fernando
Publication year - 1988
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/yea.320040105
Subject(s) - isocitrate lyase , biology , glyoxylate cycle , enzyme , biochemistry , lyase , molecular mass , isocitrate dehydrogenase , saccharomyces cerevisiae , yeast
Isocitrate lyase purified to homogeneity from Saccharomyces cerevisiae was composed of four identical subunits with a molecular mass 75 K Da. The enzyme was most active at pH 7.0 in the presence of 5 m M ‐Mg 2+ . The K m value for threo ‐ D s ‐isocitrate was 1.4 m M . Isocitrate lyase was shown to be thermostable at 50°C for 60 min at a high salt concentration, but rapidly lost activity at −20°C or by dialysis.
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