Detection of intracellular forms of secretory aspartic proteinase in Candida albicans.
The extracellular proteinase (EPR) of Candida albicans was induced in a medium containing bovine serum albumin as sole nitrogen source. There were two intracellular forms in cells induced to produce EPR, a 43 kDa protein (EPR) and a 45 kDa protein (cross-reacting material of EPR; CRM-EPR); these were detected by immunoblotting using anti-EPR antiserum. The 43 kDa protein (EPR) may be the same as the extracellular form judging by molecular mass, and the 45 kDa protein (CRM-EPR) may be a precursor form of EPR. Many dense granules were observed by electron microscopy near the plasma membrane of the mother cells in EPR-producing cells. Both the 43 and 45 kDa proteins were recovered in a membrane fraction and were solubilized by Triton X-100. When the membrane fraction was further fractionated by sucrose density gradient centrifugation, the 43 and 45 kDa proteins were differentially fractionated. This suggests that they were located in different membrane-bound structures and is consistent with an assumption that the 45 kDa protein is a precursor for EPR.
Homma
M
M
Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Japan.
Kanbe
T
T
Chibana
H
H
Tanaka
K
K
D016282:Aspartic Acid Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D002176:Candida albicans / Q000201:enzymology* / Q000648:ultrastructure; D002499:Centrifugation, Density Gradient; D003429:Cross Reactions; D004790:Enzyme Induction; D008566:Membranes / Q000187:drug effects / Q000201:enzymology; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology
D012710:Serum Albumin, Bovine; D011092:Polyethylene Glycols; D017830:Octoxynol; D016282:Aspartic Acid Endopeptidases