. "Isocitrate lyase purified to homogeneity from Saccharomyces cerevisiae was composed of four identical subunits with a molecular mass of 75 kDa. The enzyme was most active at pH 7.0 in the presence of 5 mM-Mg2+. The Km value for threo-Ds-isocitrate was 1.4 mM. Isocitrate lyase was shown to be thermostable at 50 degrees C for 60 min at a high salt concentration, but rapidly lost activity at -20 degrees C or by dialysis." . . "Yeast" . "Moreno F." . "Herrero P." . "Fernandez R." . "Lopez-Boado Y.S." . "Fernandez M.-T." . "1988"^^ . "41-46" . "Purification of isocitrate lyase from Saccharomyces cerevisiae." . "4" . "doi:10.1002/yea.320040105" .