Purification and some properties of Candida albicans DNA polymerases.
DNA polymerases of Candida albicans were purified to near homogeneity. Three well distinguished peaks of DNA polymerase activity (Enzyme I, II and III respectively) were obtained by DEAE-Sephacel chromatography. This purification step was followed by column chromatographies on Sepharose 6B and denatured DNA-cellulose. The enzymes' molecular mass and biochemical properties, including their inhibition by aphidicolin, were studied. Molecular mass was determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and was found to be 110 kDa for Enzyme I, 80 kDa for Enzyme II and 50 kDa for Enzyme III.
Jakab
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Department of Chemotherapeutical Research, BIOGAL Pharmeceutical Works, Debrecen, Hungary.
Schmidt
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Hernádi
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D016590:Aphidicolin / Q000494:pharmacology; D002176:Candida albicans / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004256:DNA Polymerase I / Q000737:chemistry / Q000302:isolation & purification; D004257:DNA Polymerase II / Q000737:chemistry / Q000302:isolation & purification; D004258:DNA Polymerase III / Q000737:chemistry / Q000302:isolation & purification; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight
D016590:Aphidicolin; D004256:DNA Polymerase I; D004257:DNA Polymerase II; D004258:DNA Polymerase III; D004259:DNA-Directed DNA Polymerase