A simple method for purification of epoxide hydratase from rat liver
- 1 May 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 163 (2) , 381-383
- https://doi.org/10.1042/bj1630381
Abstract
Rat liver epoxide hydratase was purified 460-fold to homogeneity by detergent solubilization and ion-exchange chromatography. The enzyme obtained in high yield (36%) exhibited a specific activity of 479nmol of styrene glycol formed/min per mg of protein, with styrene oxide as substrate. Only one polypeptide-staining band, mol.wt. 49500, was visible after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis.This publication has 10 references indexed in Scilit:
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