title: Structural analysis of the rat uricase gene and evidence that lysine 164 is involved in the substrate-binding site of the enzyme.
authors.affiliation: Laboratory of Biology, Saga Medical School, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Ito
authors.forename: M
authors.initials: M
authors.lastname: Nakamura
authors.forename: S
authors.initials: S
authors.lastname: Kato
authors.forename: H
authors.initials: H
authors.lastname: Ogawa
authors.forename: Y
authors.initials: Y
authors.lastname: Takagi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular / Q000379:methods; D003360:Cosmids; D004926:Escherichia coli / Q000235:genetics; D015698:Genomic Library; D007700:Kinetics; D008239:Lysine; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides; D051381:Rats; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D014503:Urate Oxidase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D019820:Xanthine; D014970:Xanthines / Q000378:metabolism
chemical_list: D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins; D014970:Xanthines; D019820:Xanthine; D014503:Urate Oxidase; D008239:Lysine