Partial purification of (1,3)-beta-glucan synthase from Candida albicans

FEMS Microbiol Lett. 1997 Jan 15;146(2):255-61. doi: 10.1111/j.1574-6968.1997.tb10202.x.


(1,3)-beta-Glucan synthase from Candida albicans was solubilized from microsomal membranes using the detergent 3-[(3-cholamidopropyl) dimethylammonio]-1-propane sulfonate (Chaps). Effective solubilization was dependent upon the strain and the method used to detect enzyme activity. The solubilized enzyme was purified over 765-fold using a modified product entrapment technique. Bovine serum albumin, an activator of glucan synthase, precipitated proteins during product entrapment and was replaced with BSA immobilized on agarose beads. SDS-PAGE analysis revealed a prominent 187-kDa band present in the product entrapped pellet as well as several additional polypeptides at 227, and 187, 182 and 39 kDa which were not prevalent in crude preparations.

MeSH terms

  • Candida albicans / enzymology*
  • Detergents
  • Electrophoresis, Polyacrylamide Gel
  • Glucosyltransferases / isolation & purification*
  • Glucosyltransferases / metabolism
  • Membrane Proteins*
  • Microsomes / enzymology
  • Schizosaccharomyces pombe Proteins*
  • Solubility


  • Detergents
  • Membrane Proteins
  • Schizosaccharomyces pombe Proteins
  • Glucosyltransferases
  • 1,3-beta-glucan synthase