Leukotriene A4 hydrolase from guinea pig lung: the presence of two catalytically active forms.
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.
Bito
H
H
Department of Physiological Chemistry and Nutrition, Faculty of Medicine, University of Tokyo.
Ohishi
N
N
Miki
I
I
Minami
M
M
Tanabe
T
T
Shimizu
T
T
Seyama
Y
Y
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
D000596:Amino Acids; D013439:Sulfhydryl Reagents; D004851:Epoxide Hydrolases; C043134:leukotriene A4 hydrolase