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  • 1. Monegal, A.
    et al.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Planas, A.
    Enzymatic characterization of bovine alpha-1,3-galactosyltransferase. Validation of a radiometric assay and kinetic mechanism2005In: Afinidad, ISSN 0001-9704, Vol. 62, no 519, p. 505-512Article in journal (Refereed)
    Abstract [es]

    alpha 3-Galactosyltransferase (alpha 3GT) transfers galactose from UDP-Gal (sugar nucleotide donor) to the N-acetyllactosaminyl or lactosyl terminal groups of glycoproteins and glycolipids, catalyzing the formation of an alpha-1,3 glycosidic bond. The terminal saccharide Gal alpha 3NAcGal beta 4Glu-R is the main antigenic determinant responsible of the hyperaccute rejection in xenotransplantation. A radiometric assay for the determination of alpha 3GT activity is implemented and validated. The recombinant enzyme (catalytic domain) expressed in Eschericia coli follows a bi bi sequential ordered kinetic mechanism with binding of donor substrate (UDP-Gal) first and acceptor substrate to form a productive ternary complex. K-M values are 30 mu M for UDP-Gal, and 1.2 mM for lactose.

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