Analysis of secreted aspartic proteinases from Candida albicans: purification and characterization of individual Sap1, Sap2 and Sap3 isoenzymes
Article Abstract:
The biochemical properties of secreted aspartic proteinase isoenzymes (Sap1, Sap2 and Sap3) and the method of purification for each isoenzyme were analyzed. A simple purification protocol was employed to monitor Saps 1,2 and 3 in culture filtrates and to recover individual Sap products. Substrate specificity, pH profile and thermal stability of each isoenzyme were evaluated by gel electrophoresis, immunoblotting and proteinase assays. There was no major difference in specificity among the isoenzymes. Sap 3 has more activity at low pH and has a higher thermal stability than Saps 1 and 2.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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3-Phosphoglycerate kinase: a glycolytic enzyme protein present in the cell wall of Candida albicans
Article Abstract:
3-Phosphoglycerate kinase (PGK) was confirmed to be a genuine cell wall protein of Candida albicans using different methods such as indirect immunofluorescence, immunoelectron microscopy and northern blot analysis. A 40 kDa protein was identified by monovalent affinity-purified antibody to the fusion protein specified by the cDNA clone. The nucleotide sequence of PGK was found to be similar to those of Candida maltosa, Kluyveromyces lactis and Saccharomyces cerevisiae.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Functional reconstitution of a purified proline permease from Candida albicans: interaction with the antifungal cispentacin
Article Abstract:
The purification of proline permease from Candida albicans to homogeneity and its functional reconstitution into proteoliposomes were assessed for the first time. The purified proline permease produced two bands (67 and 64 kDa) using SDS-PAGE. However, a single band of 67 kDa was produced by native PAGE and Western blotting. The antifungal cispentacin competitively inhibits the binding and translocation of L-proline in reconstituted proteoliposomes.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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