Abstract
The enzymes catalyzing the synthesis and hydrolysis of cholesteryl esters were studied in the acetone dry powder of normal aorta of male rat and rabbit. In both species the enzymes were found to have similar stability, solubility and kinetic properties. The synthetic enzyme was found to be most effective with an emulsified substrate and had a pH maximum of 6.2. Exogeneous ATP or CoA did not stimulate the activity. Sodium taurocholate was essential for activity but was found inhibitory at higher concentrations. The hydrolytic enzyme was about three times more effective when using a micellar substrate than for the emulsified substrate. The enzyme preparation exhibited two pH optima for hydrolysis, depending upon the physical state of the substrate. The micellar substrate was optimally hydrolyzed at pH 6.6 and the albumin dispersed substrate at pH 7.4. In the rat aorta preparation, the specific activities for hydrolysis and synthesis were 9.5 and 5.7, respectively; in the rabbit they were 3.0 and 3.3, respectively.
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