Abstract
Efficiency of substrates for cholesterol esterase (EC 3.1.1.13) assay, and regulation of the activity were investigated in rat epididymal adipose tissue. The activity in the supernatant was activated by cyclic AMP-dependent protein kinase, cyclic AMP, ATP and Mg 2+, both with micellar and liposomal substrates. However, the micellar substrate was more suitable for the assay than the liposomal with respect to V max and K m . Thus, the micellar substrate was employed. Pretreatment of the supernatant with exogenous cyclic AMP-dependent protein kinase enhanced the activity dose dependency, whereas that with cyclic AMP decreased the activity slightly. The cyclic AMP-dependent protein kinase activity in the assay mixture was within the range which can cause changes in cholesterol esterase activity. These results suggest that the amount of cyclic AMP-dependent protein kinase, rather than the cyclic AMP level, plays an important role in the regulation of cholesterol esterase in tissues with a high cholesterol esterase activity relative to the kinase activity, such as in adipose tissue.
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