Hydrolysis of chylomicron retinyl ester by an acid retinyl esterase of rat liver
Rat liver homogenate hydrolyzed chylomicron remnant retinyl esters with pH optima 4.5, 6 and 8. The retinyl ester hydrolysis at pH 4.5 was correlated to the acid phosphatase activity in different subcellular fractions, and thus the highest activity was found in highly purified lysosomes. These fractions could also catalyze the reverse reaction, i.e., the esterification of retinol when incubated wi