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  • Title: Identification and characterization of N-acetylglucosamine-6-O-sulfate-specific beta1,4-galactosyltransferase in human colorectal mucosa.
    Author: Seko A, Hara-Kuge S, Yonezawa S, Nagata K, Yamashita K.
    Journal: FEBS Lett; 1998 Dec 04; 440(3):307-10. PubMed ID: 9872392.
    Abstract:
    6-Sulfo-sialyl Lewis X structure is attributable to recognition between lymphocytes and high endothelial venules. However, the biosynthetic pathway still remains unclear. We found that a beta-galactosyltransferase (betaGalT) in human colorectal mucosa preferentially acts on GlcNAc-6-O-sulfate (6S-GN). 6S-GN:beta4GalT was partially purified by UDP-hexanolamine-Sepharose and asialo-agalacto-ovomucin-Sepharose chromatographies. The optimum pH of this enzyme was found to be 6.5-7.5 and the Michaelis constants for 6S-GN and UDP-Gal were 0.43 mM and 16 microM, respectively. The enzymatic activity was dependent on divalent cations and the substrate specificity was not affected by alpha-lactalbumin. This is the first demonstration of the occurrence of 6S-GN:beta4GalT.
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