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Purification of native enolase from medically important Candida species
Author(s) -
Ballantyne Denis S.,
Warmington John R.
Publication year - 2000
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba19990106
Subject(s) - enolase , candida albicans , biology , yeast , antigen , enzyme , biochemistry , microbiology and biotechnology , immunology , immunohistochemistry
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.