Abstract
The enzyme, mutarotase, has been purified from hog kidney cortex, using DEAE-cellulose chromatography and Sephadex G-75 filtration. The preparation, studied with the analytical ultracentrifuge, has an s 20 value of 3.40S. Using the method of rapid attainment of sedimentation equilibrium with a short column, the apparent molecular weight has been determined as 54,300 ± 4000. The pH-activity curve of this enzyme shows a broad optimum in the neighborhood of pH 7.0.
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