Abstract
A microsomal epoxide hydrase, which catalyzes the hydration of styrene oxide to form styrene glycol, has been purified from guinea pig liver. Solubilization from microsomes with cutscum and further purification by (NH 4) 2SO 4 precipitation, Sephadex G-25 chromatography, and calcium phosphate gel adsorption and desorption resulted in an overall 40-fold increase in specific activity. The solubilized enzyme was very unstable but stability was recovered after the last purification step. The K m and ν max of the purified enzyme for styrene oxide are 5.3 · 10 −4 M and 2.70μmoles product per mg nitrogen per 5 min, respectively. No cofactors are required. The enzyme is not inhibited by the product styrene glycol or by EDTA and is slightly inhibited by sulfhydryl reagents. The pH optimum is 8–9. The purified preparation catalyzes the enzymatic hydration of a variety of epoxides.
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