3, PHD,DASP3.1. You can also download agent from ds150e vci.Human sialyltransferases as potential biocatalysts: characterization of the human ST6Gal I (alpha2,6-sialyltransferase) gene and the production of oligosaccharide structures by recombinant human ST6Gal I in a baculovirus expression system.
Previously we have characterized the human polypeptide (ST6Gal I) that catalyzes the alpha2,6-sialylation of terminal N-acetylglucosamine residues and a corresponding nucleic acid (ST6Gal I cDNA) that encodes the human polypeptide (ST6Gal I). The cDNA for ST6Gal I was inserted into a baculovirus expression vector and used to infect Sf9 insect cells. Biochemical characterization of the enzyme expressed in the insect cells showed that ST6Gal I was active and produced the same alpha2,6-sialylation product as the recombinant polypeptide in vitro. The nucleic acid and polypeptide were immunologically cross-reactive with antibodies that specifically recognize the rat (RnST6Gal I) and chicken (GnST6Gal I) enzyme. These results were the first demonstration of the structural and immunologic identity of a mammalian sialyltransferase and its corresponding nucleic acid. In the present study, we further characterized the human ST6Gal I gene. Using a full-length cDNA probe generated from the recombinant cDNA of ST6Gal I and a partial-length cDNA probe generated from the ST6Gal I gene, we isolated genomic clones containing ST6Gal I. Analysis of these genomic clones revealed an ST6Gal I gene of 9.4 kilobases (kb) that was composed of 13 exons and 12 introns. The ST6Gal I gene had a nucleotide sequence highly homologous to the rat (RnST6Gal I) and chicken (GnST6Gal I) gene, with 90.6 and 88.1% homology, respectively. The genomic structure of the human ST6Gal I gene was also compared to the genomic structure of the RnST6Gal I and GnST6Gal I gene. The comparison showed that the human ST6Gal I gene had 2 kb of a 5'-flanking region, 8 kb of a
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