Leukotriene A4 hydrolase from guinea pig lung: the presence of two catalytically active forms |
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| Authors: | H Bito N Ohishi I Miki M Minami T Tanabe T Shimizu Y Seyama |
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| Affiliation: | Department of Physiological Chemistry and Nutrition, Faculty of Medicine, University of Tokyo. |
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| 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. |
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