Electrophoretic Detection of Cytoplasmic Serine Proteinases (Gelatinases) in Candida albicans

Abstract Rodier, M.-H., El Moudni, B., Ghazali, M., Lacroix, C., and Jacquemin, J.-L. 1994. Electrophoretic detection of cytoplasmic serine proteinases (gelatinases) in Candida albicans. Experimental Mycology 18: 267-270. Proteolytic activities of Candida albicans were identified using sodium dodecyl sulfate-polyacrylamide gel electrophoresis with gels containing gelatin as proteinase substrate. Cytoplasmic extracts of five isolates were tested with this method. Two major proteolytic activities of Mr 50,000 and 60,000 were conserved between isolates whereas two other less intense activities of Mr 90,000 and 120,000 were only detected in three isolates. The two bands of proteolysis of Mr, 50,000 and 60,000 were revealed between pH 5.0 and pH 8.0, optimally active at pH 7.0, and their isoelectric point was 4.5. They were not influenced by the presence of 2-mercaptoethanol. Their sensitivity to phenylmethylsulfonyl fluoride and chymostatin allowed them to be characterized as serine proteinases. These two neutral proteinases were not secreted in culture supernatant.