Purification of native enolase from medically important Candida species.
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.
Ballantyne
D S
DS
School of Biomedical Sciences, Curtin University of Technology, GPO Box U1987, Perth WA 6845, Australia.
Warmington
J R
JR
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*
D010751:Phosphopyruvate Hydratase