Several rat liver microsomal esterases have been isolated. One of these was purified to homogeneity and its physical and catalytic properties were investigated. The enzyme is composed of two subunits of equal molecular weight. Each 70,000 molecular weight subunit appears to have an active site. Evidence is presented which suggests that catalysis involves the formation of an acyl-enzyme intermediate and requires the presence of an unprotonated residue with a pK of about 6.0.
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Haugen et al. (1974) studied this question.
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