Banerjee, AGanesan, KDatta, A1991-10-012009-05-271991-10-012009-05-271991-10-01Banerjee A, Ganesan K, Datta A. Rapid purification of secretory acid proteinase from Candida albicans and its characterization. Indian Journal of Biochemistry & Biophysics. 1991 Oct-Dec; 28(5-6): 444-8http://imsear.searo.who.int/handle/123456789/28344Secretory acid proteinase from C. albicans was purified from culture supernatant to apparent homogeneity by ion-exchange chromatography. Two isozymes of the proteinase were resolved using a novel chromatofocusing method. The enzyme, which appears to be a glycoprotein, consists of a single polypeptide chain with glutamine at the N-terminus. Its molecular weight is about 45,000 and isoelectric point is pH 4.6. At pH 5, the proteinase is stable at 45 degrees C for at least 15 min. It has a broad substrate specificity. With BSA as a substrate, Km was determined to be 1.6 x 10(-4) M. The enzyme is inhibited by pepstatin and thus is a carboxyl proteinase. It undergoes autocatalytic digestion at or below pH 5.0. The kinetics of induction of proteinase by various proteins are also reported.engAmino Acids --analysisCandida albicans --enzymologyEndopeptidases --isolation & purificationIsoelectric PointIsoenzymes --isolation & purificationKineticsMolecular WeightRapid purification of secretory acid proteinase from Candida albicans and its characterization.Journal Article