title: Chromatographic purification and homogeneity of extracellular acid proteinase of Aspergillus Fumigatus.
abstract: The extracellular acid proteinase from A. fumigatus was purified by employing several chromatographic procedures and a 164 fold purification with 22% yield was achieved. The homogeneity of the enzyme was confirmed by SDS-Polyacrylamide gel electrophoresis, immodiffusion and immunoelectrophoresis techniques.
mesh_terms: D016282:Aspartic Acid Endopeptidases; D001232:Aspergillus fumigatus / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000276:immunology / Q000302:isolation & purification*; D005110:Extracellular Space / Q000201:enzymology
chemical_list: D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C026442:Aspergillus acid proteinase