Identification and partial characterization of two proteinases from the cell envelope of Candida albicans blastospores.
As we have communicated previously, the fungal opportunist Candida albicans produces an angiotensin-1 liberating proteinase and a serine proteinase that acts as a converter of the coagulation factor X in vitro (25). Both enzymes are attached to delipidated cell fragments of fungal blastospores. They copurify upon ion exchange chromatography and gel filtration. The enzymes could be separated by hydrophobic chromatography on Phenylsepharose. According to their substrate and inhibition pattern, the enzymes have been classified as an aspartyl proteinase and a chymotrypsin-like proteinase. Their partial characterization includes estimates of the molecular weight and isoelectric points.
D002176:Candida albicans / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D007525:Isoelectric Focusing; D007700:Kinetics; D008565:Membrane Proteins / Q000302:isolation & purification; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D013172:Spores, Fungal / Q000201:enzymology; D013379:Substrate Specificity
D008565:Membrane Proteins; D010447:Peptide Hydrolases