The 48 kDa glycolytic enzyme, enolase, has been identified as an immunodomi
nant 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-excha
nge chromatography method that was preceded by an organic extraction. The e
nolases purified by this method have a high specific activity and the proce
dure is 40% efficient, with an average of 5 mg of enolase/g of Candida cell
s. The purification of native enolase from medically important Candida spec
ies will enable the immunological significance and interspecies relationshi
ps of this major fungal antigen to be investigated.