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- W2089969444 abstract "Endo-N-acetyl-β-d-glucosaminidase H (Endo H) was purified to homogeneity (3000-fold) from a culture filtrate of Streptomyces plicatus. The key step was substrate-affinity chromatography, which afforded a 1000-fold purification and yielded a protease- and exoglycosidase-free preparation of Endo H. Proteins from the crude sample were applied to the substrate-affinity column, consisting of yeast-invertase glycopeptides bound to Sepharose-immobilized concanavalin A. After washing off the unbound proteins, Endo H was quantitatively eluted by methyl α-d-mannopyranoside. Various conditions were tested to achieve an optimal binding of Endo H to this substrate-affinity gel. After substrate-affinity chromatography, Endo H was separated from the coeluted glycopeptide substrate and some protein impurities by gel filtration and hydrophobic chromatography." @default.
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- W2089969444 date "1989-06-01" @default.
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- W2089969444 title "Purification of endo-N-acetyl-β-d-glucosaminidase H by substrate-affinity chromatography" @default.
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- W2089969444 doi "https://doi.org/10.1016/0008-6215(89)84105-9" @default.
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