Purification of native enolase from medically important Candida species

Citation
Ds. Ballantyne et Jr. Warmington, Purification of native enolase from medically important Candida species, BIOT APP B, 31, 2000, pp. 213-218
Citations number
24
Categorie Soggetti
Biotecnology & Applied Microbiology","Biochemistry & Biophysics
Journal title
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
ISSN journal
08854513 → ACNP
Volume
31
Year of publication
2000
Part
3
Pages
213 - 218
Database
ISI
SICI code
0885-4513(200006)31:<213:PONEFM>2.0.ZU;2-Q
Abstract
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.