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 70kDa 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...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1989-02, Vol.105 (2), p.261-264
Main Authors: Bito, Haruhiko, Ohishi, Nobuya, Miki, Ichiro, Minami, Michiko, Tanabe, Tadashi, Shimizu, Takao, Seyama, Yousuke
Format: Article
Language:English
Subjects:
Amino Acids - analysis
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Chromatography, Ion Exchange
Enzymes and enzyme inhibitors
Epoxide Hydrolases - analysis
Epoxide Hydrolases - isolation & purification
Epoxide Hydrolases - metabolism
Female
Fundamental and applied biological sciences. Psychology
Guinea Pigs
Hydrolases
Isoelectric Focusing
Lung - enzymology
Male
Molecular Weight
Sulfhydryl Reagents
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Summary:Leukotriene A4 hydrolase was purified to apparent homogeneity from the guinea pig lung. The molecular weight was determined to be 70kDa 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 IIe-3 and Ser-14 (human) by Val-3 and Thr-14 (guinea pig), respectively.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122650