Mercier M, Forget A, Grolier P, Azais-Braesco V
Food, Food safety laboratory, INRA-CRJ, Jouy-en-Josas, France.
Biochim Biophys Acta. 1994 May 13;1212(2):176-82. doi: 10.1016/0005-2760(94)90251-8.
When incorporated into liposomes made of phospholipids, retinyl palmitate is an adequate substrate for an acidic REH (aREH). In rat liver, this activity is mainly localized in the lysosomal fraction. Kinetic parameters have been determined for retinyl palmitate (Km = 315 microM; maximal rate = 22.1 nmol retinol/h per mg protein). The aREH activity is different from the lysosomal acidic cholesteryl ester hydrolase (aCEH): cholesteryl oleate does not inhibit aREH activity, neither do some aCEH specific inhibitors, and aREH does not hydrolyse cholesteryl ester. Involvement of aREH in the hydrolysis of lipid droplets retinyl esters in fat storing cells is discussed.
当视黄醇棕榈酸酯掺入由磷脂制成的脂质体中时，它是酸性视黄醇酯水解酶（aREH）的合适底物。在大鼠肝脏中，这种活性主要定位于溶酶体部分。已确定视黄醇棕榈酸酯的动力学参数（Km = 315 microM；最大速率 = 22.1 nmol视黄醇/小时/毫克蛋白质）。aREH活性不同于溶酶体酸性胆固醇酯水解酶（aCEH）：油酸胆固醇酯不抑制aREH活性，一些aCEH特异性抑制剂也不抑制，且aREH不水解胆固醇酯。本文讨论了aREH在脂肪储存细胞中脂质滴视黄醇酯水解中的作用。
