[Purification, characterization and reverse cholesterol transport of human serum apolipoprotein A-IV]

In order to study the function of apoA-IV, human serum apoA-IV was isolated and purified. LDS was isolated with NaBr density gradient ultracentrifugation and then incubated with intralipid according to the method of Weinberg and Scanu. Protein complex containing apoA-IV was obtained. The apo-IV was purified from protein complex by preparative SDS-PAGE, electroelution and removal of SDS. ApoA-IV thus prepared gave a single band on SDS-PAGE with a MW of 46 kD. Amino acid composition and isoelectric focusing pI (5.27 and 5.47) of apoA-IV were similar to those reported in the literature. The effects of apoA-IV and liposome (apoA-IV: DMPC) on cholesterol efflux from hum skin fibroblast were studied. There was no significant difference (P > 0.5) between apoA-IV and control but a very significant difference (P < 0.001) between liposome (apoA-IV:DMPC) and control, suggesting that liposomes (apoA-IV:DMPC) play a role in reverse cholesterol transport. The results may offer a new approach for the prevention and treatment of atherosclerotic coronary heart disease.