Abstract
The soluble proteins of the particulate and the supernatant fractions of the rat-liver cells have been separated into a number of enzyme peaks by DEAE-cellulose chromatography. By a technique using Sephadex G-50, the capacity of each Chromatographie fraction to bind radioactive diwopropyl phosphorofluoridate (DF 32P) has been determined and correlated to its esterase activity towards some phenyl, ethyl and glyceryl esters. It is found that fractions having the maximal esterase activity exactly coincide with those with the highest DF 32P-binding capacity. Except for one peak in the supernatant fraction, all other esterase peaks take up the radioactive label and there are no radioactive peaks without esterase activity. The esterase peaks show some broad differences in their relative capacity to hydrolyze simple esters. The microsomal fraction has the highest esterase and DF 32P-binding activity. Though the unfractionated cell components exhibit some activity towards choline esters, this is not found to be localized in anv of the esterase peaks obtained bv DEAE-cellulose chromatography.
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