title: Purification of native enolase from medically important Candida species.
abstract: The 48 kDa glycolytic enzyme, enolase, has been identified as an immunodominant antigen in Candida albicans infections. It has also been identified as an important fungal allergen. Enolase from a number of medically important Candida species has been purified using a two-step anion- and cation-exchange chromatography method that was preceded by an organic extraction. The enolases purified by this method have a high specific activity and the procedure is 40% efficient, with an average of 5 mg of enolase/g of Candida cells. The purification of native enolase from medically important Candida species will enable the immunological significance and interspecies relationships of this major fungal antigen to be investigated.
authors.affiliation: School of Biomedical Sciences, Curtin University of Technology, GPO Box U1987, Perth WA 6845, Australia.
authors.forename: D S
authors.initials: DS
authors.lastname: Ballantyne
authors.forename: J R
authors.initials: JR
authors.lastname: Warmington
mesh_terms: D002175:Candida / Q000201:enzymology*; D005591:Chemical Fractionation; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D010751:Phosphopyruvate Hydratase / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D010751:Phosphopyruvate Hydratase