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Purification of isocitrate lyase from Saccharomyces cerevisiae
Y S Lopez-Boado1, P Herrero, M T Fernandez
1Departamento de Biología Funcional, Facultad de Medicina, Universidad de Oviedo, Spain.
Yeast (Chichester, England)
|March 1, 1988
Abstract:
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.