title: Molecular cloning of human beta 1,4-galactosyltransferase and expression of catalytic activity of the fusion protein in Escherichia coli.
abstract: 1. Three groups of cDNA clones (total of six) for human UDP-galactose: beta N-acetylglucosamine galactosyltransferase (4 beta GT) were obtained by screening of a fetal liver library in lambda gt11 with an affinity purified anti4 beta GT antibody. 2. One group of clones (three clones) reacted with two distinct anti4 beta GT murine monoclonal antibodies. 3. Nucleotide sequence of this group of clones were similar to published sequence for human 4 beta GTcDNA, except the 74 nucleotides at the 5'-end. 4. Partially purified fusion protein encoded by this group of clones showed all the catalytic properties of 4 beta GT, although the cDNA was partial and the protein was probably unglycosylated.
authors.affiliation: Department of Gynecologic Oncology, Roswell Park Cancer Institute, Buffalo, NY 14263.
authors.forename: S K
authors.initials: SK
authors.lastname: Chatterjee
mesh_terms: D000911:Antibodies, Monoclonal; D002384:Catalysis; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D006801:Humans; D007163:Immunosorbent Techniques; D009237:N-Acetyllactosamine Synthase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D011993:Recombinant Fusion Proteins; D004247:DNA; D009237:N-Acetyllactosamine Synthase