title: Molecular cloning and expression of mouse leukotriene A4 hydrolase cDNA.
abstract: A cDNA clone for mouse leukotriene A4 hydrolase encoding the full sequence of the enzyme was isolated from a mouse spleen lambda ZAP-II library. The identification was ascertained by expression of enzyme activity in Escherichia coli. The encoded protein has 610 amino acids and exhibits an extensive identity (93%) with the human leukotriene A4 hydrolase. A region spanning between residues 233 and 340, where the zinc binding site is located, was found to be perfectly conserved between the two species. We found six sites of polymorphism in the cDNA sequence of mouse LTA4 hydrolase, one of which leads to a difference in the encoded amino acid. The polymorphism of cDNA was confirmed by reverse transcription-PCR sequencing of mouse spleen total RNA, prepared as a mixture from ten different strains.
authors.affiliation: Department of Physiological Chemistry, Karolinska Institutet, Stockholm, Sweden.
authors.forename: J F
authors.initials: JF
authors.lastname: Medina
authors.forename: O
authors.initials: O
authors.lastname: Rådmark
authors.forename: C D
authors.initials: CD
authors.lastname: Funk
authors.forename: J Z
authors.initials: JZ
authors.lastname: Haeggström
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular / Q000379:methods; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D004851:Epoxide Hydrolases / Q000096:biosynthesis / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D015723:Gene Library; D007700:Kinetics; D051379:Mice; D008969:Molecular Sequence Data; D010957:Plasmids; D016133:Polymerase Chain Reaction / Q000379:methods; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis; D015183:Restriction Mapping; D013154:Spleen / Q000201:enzymology
chemical_list: D011994:Recombinant Proteins; D004247:DNA; D012194:RNA-Directed DNA Polymerase; D004851:Epoxide Hydrolases; C043134:leukotriene A4 hydrolase