Abstract
Summary
By repeated continuous flow curtain electrophoresis of human serum, 2 distinct phenyl acetate hydrolyzing esterases were purified 120 and 850 times. One esterase was heat-labile and inactivated by EDTA, while the other was heat-stable and required EDTA for activity. EDTA-inactivation could be prevented by manganese. The methods for purification and assay are described and the results discussed.
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