Characterization of Acetyl Low-density Lipoprotein Receptor from Rat Liver

Abstract

The receptor for acetyl low-density lipoprotein (Ac-LDL) was partially purified from rat liver membrane. Using 40mM octyl-glucoside buffer, Ac-LDL receptor was solubilized from liver membrane, and was partially purified using maleyl bovine serum albumin affinity column, which is a potent inhibitor of Ac-LDL binding. The K_d for membrane or partially purified receptor was about 3-4μg/ml. The receptor had apparent Mr. 249, 000 and pI 6.1.