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  • Title: Purification and characterization of alpha (2-6)-sialyltransferase from human liver.
    Author: Sticher U, Gross HJ, Brossmer R.
    Journal: Glycoconj J; 1991 Feb; 8(1):45-54. PubMed ID: 1823612.
    Abstract:
    A Gal beta 1-4GlcNAc alpha (2-6)-sialyltransferase from human liver was purified 34,340-fold with 18% yield by dye chromatography on Cibacron Blue F3GA and cation exchange FPLC. The enzyme preparation was free of other sialyltransferases. It did not contain CMP-NeuAc hydrolase, protease, or sialidase activity, and was stable at -20 degrees C for at least eight months. The donor substrate specificity was examined with CMP-NeuAc analogues modified at C-5 or C-9 of the N-acetylneuraminic acid moiety. Affinity of the human enzyme for parent CMP-NeuAc and each CMP-NeuAc analogue was substantially higher than the corresponding Gal beta 1-4GlcNAc alpha (2-6)-sialyltransferase from rat liver.
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