Coenzyme-A-dependent Esterification of Cholesterol in Rat Intestinal Mucosa

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Abstract
Rat intestinal mucosa contained an enzyme which catalyzed the esterification of cholesterol. The enzyme was CoA-dependent and probably an acyl-CoA: cholesterol acyltransferase (ACAT) (E.C.2.3.1.26). Maximal activity in vitro was obtained when long chain acylcarnitines, CoA and carnitine palmityltransferase were used as an acyl-CoA generating system. The enzyme was localized in the microsomal fraction, had a pH optimum between 6.4-7.2, and oleate was the preferred acyl group. The activity of the enzyme was highest in the proximal jejunum and had a capacity that could account for all cholesteryl esters found in intestinal rat lymph.