Nonspecific acid phosphatase from Schizosaccharomyces pombe. Purification and physical chemical properties.

摘要: Repressible nonspecific acid phosphatase from Schizosaccharomyces pombe was purified to apparent homogeneity, as ascertained ultracentrifugal, electrophoretic, and chromatographic data. The native protein has a molecular weight of 383,000 determined by sucrose density gradient centrifugation 381,000 gel filtration. can be dissociated in the presence 8 M urea-1% sodium dodecyl sulfate into sub-units possessing an approximate 104,000. Neutral sugars account for about 66% total contribute high solubility some other physical properties this enzyme. Purified enzyme preparations have Km 4-nitrophenyl phosphate 0.17 mM broad substrate specificity, but do not show diesterase activity. Phosphate are competitive inhibitors. is inactivated at neutral alkaline pH relatively low temperatures. Mannose galactose found main components carbohydrate moiety; glucosamine present lower amounts. amino analysis revealed content aspartate, threonine, serine; no sulfhydryl group could detected. Pi released stoichiometric amount (1 mol per monomer) on digestion.