title: Purification of isocitrate lyase from Saccharomyces cerevisiae.
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.
authors.affiliation: Departamento de Biología Funcional, Facultad de Medicina, Universidad de Oviedo, Spain.
authors.forename: Y S
authors.initials: YS
authors.lastname: Lopez-Boado
authors.forename: P
authors.initials: P
authors.lastname: Herrero
authors.forename: M T
authors.initials: MT
authors.lastname: Fernandez
authors.forename: R
authors.initials: R
authors.lastname: Fernandez
authors.forename: F
authors.initials: F
authors.lastname: Moreno
mesh_terms: D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007522:Isocitrate Lyase / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D007652:Oxo-Acid-Lyases / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
chemical_list: D007652:Oxo-Acid-Lyases; D007522:Isocitrate Lyase