Retinyl ester hydrolase and the visual cycle in the chicken eye

Abstract

The ability of chicken retina and retinal pigment epithelium (RPE) membrane to hydrolyze vitamin A esters ([9,10(-3)H]all-trans- and 11-cis-retinyl palmitate) was studied. Hydrolytic activity within the retina was optimal at acidic pH of 5.0, whereas in the RPE significant hydrolytic activity was exhibited over a broad range of hydrogen ion concentrations. The highest rate of hydrolysis was associated with the all-trans-isomer and located within retina and RPE membranes [the apparent maximal velocity (Vmax) and Michaelis-Menten constant (Km) were 770 pmol.min.-1.mg-1 and 45 microM and 300 pmol.min-1.mg-1 and 3.6 microM, respectively[. Retinyl ester hydrolase activities for 11-cis-retinyl palmitate in the retina and RPE were correspondingly lower (apparent Vmax of 204 pmol.min.-1.mg-1 and Km of 18.5 microM in the retina; apparent Vmax of 131 pmol.min.-1.mg-1 and Km of 4 microM in the RPE). Together with results from other laboratories, results from the present study suggest that chicken retina contains important enzymes to complete the visual cycle.