title: Leukotriene A4 hydrolase from guinea pig lung: the presence of two catalytically active forms.
abstract: Leukotriene A4 hydrolase was purified to apparent homogeneity from the guinea pig lung. The molecular weight was determined to be 70 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme exhibited two active forms with different pI values (5.7 and 5.4) depending on the presence or absence of SH-reducing reagents during purification procedures. No significant differences were observed between both forms of the enzyme as regards the catalytic properties. The N-terminal 20 amino acid sequence (PEVVDTXSLASPATVXRTKH) showed a 90% identity to the human enzyme with a constitutive substitution of Ile-3 and Ser-14 (human) by Val-3 and Thr-14 (guinea pig), respectively.
authors.affiliation: Department of Physiological Chemistry and Nutrition, Faculty of Medicine, University of Tokyo.
authors.forename: H
authors.initials: H
authors.lastname: Bito
authors.forename: N
authors.initials: N
authors.lastname: Ohishi
authors.forename: I
authors.initials: I
authors.lastname: Miki
authors.forename: M
authors.initials: M
authors.lastname: Minami
authors.forename: T
authors.initials: T
authors.lastname: Tanabe
authors.forename: T
authors.initials: T
authors.lastname: Shimizu
authors.forename: Y
authors.initials: Y
authors.lastname: Seyama
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002852:Chromatography, Ion Exchange; D004851:Epoxide Hydrolases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006168:Guinea Pigs; D007525:Isoelectric Focusing; D008168:Lung / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D013439:Sulfhydryl Reagents
chemical_list: D000596:Amino Acids; D013439:Sulfhydryl Reagents; D004851:Epoxide Hydrolases; C043134:leukotriene A4 hydrolase