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- W2076624279 abstract "A β-galactosidase (β-D-galactoside galactohydrolase, EC 3.2.1.23) has been isolated and purified to homogeneity from cell homogenates of cell suspension cultures of a thalloid liverwort, Marchantia polymorpha. The enzyme in 0.1 M phosphate buffer soluble protein fraction was dialyzed at pH 5.2 and further purified by a combination of chromatographic techniques including DEAE-Sephadex A-50, p-aminophenyl β-d-thiogalactopyranoside-linked Sepharose 4B and Sephadex G-200. The molecular weight of β-galactosidase by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and by Sephadex G-200 gel filtration is 62 000 and 67 000, respectively. The isoelectric point of the enzyme is found to be pH 4.2. The optimal activity occurs at pH 3.4 with McIlvaine buffer, and at pH 2.6 with glycineHCl buffer. The Km- and Vmax-values are 0.625 mM and 658 units/mg protein for p-nitrophenyl β-d-galactopyranoside. The enzyme catalyzes the transfer of the d-galactosyl residues from p-nitrophenyl β-d-galactopyranoside to d-glucose. Furthermore, the enzyme acts on the galactan extracted from citrus pectic polysaccharides in an exo-fashion." @default.
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- W2076624279 date "1986-01-01" @default.
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- W2076624279 title "Purification and characterization of β-galactosidase from cell suspension cultures of Marchantia polymorpha" @default.
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- W2076624279 doi "https://doi.org/10.1016/0168-9452(86)90077-4" @default.
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