Feb 10, 2004

Purification and characterization of a 43-kilodalton extracellular serine proteinase from Cryptococcus neoformans

Journal of Clinical Microbiology
Jae il Yoo JiBong Su Kim


An extracellular proteinase was purified from culture filtrates of Cryptococcus neoformans NHPY24 by DEAE ion-exchange chromatography and gelatin affinity column chromatography with azoalbumin as the substrate. The molecular mass of the purified enzyme was 43 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, its pH optimum was 7.0 to 8.0, and maximal activity was obtained at pH 7.5 and 37 degrees C. By isoelectric focusing, the purified enzyme had a pI of 4.77. Enzyme activity was inhibited by serine proteinase inhibitors such as phenylmethylsulfonyl fluoride and diisopropylfluorophosphate. The purified enzyme was thus a serine proteinase. It hydrolyzed natural substrates including hemoglobin, beta-casein, and gamma globulin.

Mentioned in this Paper

Expi protein, rat
Infection by Cryptococcus Neoformans
Polyacrylamide Gels
Serine Proteinase Inhibitors, Exogenous
Serine Proteinase Inhibitors

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