| Literature DB >> 869931 |
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.Entities:
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Year: 1977 PMID: 869931 PMCID: PMC1164707 DOI: 10.1042/bj1630381
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857