title: Purification and partial characterization of acid phosphatase from Candida lipolytica.
abstract: Non-specific acid phosphatase from Candida lipolytica cells was purified 111-fold by chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 and Sepharose 4B. The enzyme is a glycoprotein containing 67% neutral sugars. The molecular mass of the highly purified acid phosphatase was found to be approximately 95 kDa by both SDS-PAGE and gel filtration. The pH and temperature optima were 5.8 and 55 degrees C, respectively. The enzyme was stable at pH values between 3.5 and 5.5 and at temperatures up to 60 degrees C. The purified phosphatase had a Km value of 3.64 mM for p-nitrophenyl phosphate and showed broad substrate specificity.
authors: Institute of Microbiology, Bulgarian Academy of Sciences, Sofia.
authors: E S
authors: ES
authors: Vasileva-Tonkova
authors: D N
authors: DN
authors: Galabova
authors: M A
authors: MA
authors: Balasheva
authors: A V
authors: AV
authors: Sotirova
mesh_terms: D000135:Acid Phosphatase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002175:Candida / Q000201:enzymology*; D002241:Carbohydrates / Q000032:analysis; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D002241:Carbohydrates; D000135:Acid Phosphatase