Abstract
The kinetics of one microbial and two mammalian cholesterol esterases have been examined using a variety of aryl acetates in homogeneous solution. The mammalian enzymes behaved identically but differed somewhat from that of microbial origin. The reactions of all three were not affected by either electronic or hydrophobic characteristics. Taurocholic acid was without effect on the microbial enzyme; at low concentrations it inhibited the mammalian system, but when present in millimolar amounts notable increases in rate were discerned, attributable to the detergent effect on the enzyme.
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