Purification of isocitrate lyase from Saccharomyces cerevisiae |
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Authors: | Y S Lopez-Boado P Herrero M T Fernandez R Fernandez F Moreno |
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Affiliation: | Departamento de Biología Funcional, Facultad de Medicina, Universidad de Oviedo, Spain. |
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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. |
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Keywords: | Isocitrate lyase purification Catabolite inactivation Saccharomyces cerevisiae |
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