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- W1969847425 abstract "The catalytic subunit of a protein phosphatase 2A (PP2Ac) purified from Yarrowia lipolytica was immobilized by covalent coupling on CNBr-Sepharose 4B with a fixation yield of about 70−85%. The specific activity of free PP2Ac for substrate phosvitin was almost totally preserved by the immobilization process. The immobilized enzyme exhibits strongly improved thermostability. Phosvitin dephosphorylation by immobilized PP2Ac attained 14% and 35% yield after 3 and 17 h incubation, respectively, and resulted in modified phosvitin properties, e.g., improved solubility and alteration of ultraviolet absorption spectrum. Electrophoretic data indicated that β-phosvitin was preferentially dephosphorylated by the immobilized enzyme. Presence of a reductant such as DTT in the reaction medium improved dephosphorylation efficiency by inducing formation of a phosphate complex which would prevent enzyme inhibition by the released phosphate. This work indicates that immobilization of protein phosphatases is a performant tool to achieve modifications of highly phosphorylated proteins through dephosphorylation, with easy retrieval of the modified protein from the reaction medium. Keywords: Protein phosphatase 2A; immobilized enzyme; phosvitin dephosphorylation; yeast Yarrowia lipolytica" @default.
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- W1969847425 date "1997-08-01" @default.
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- W1969847425 title "Gel-Immobilized Protein Phosphatase 2A from <i>Yarrowia lipolytica</i> Dephosphorylates Phosvitin and Modifies Its Functional Properties" @default.
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- W1969847425 doi "https://doi.org/10.1021/jf9700790" @default.
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