Purification and characterization of two high-density-lipoprotein-binding proteins from rat and human liver

摘要: The liver plays a major role in the metabolism of plasma high-density lipoprotein (HDL). Several groups have postulated, but others refuted, existence classical membrane receptor which recognizes HDL. In present study, we identified and purified two HDL-binding proteins 120 kDa (HB1) 100 (HB2), with apparent specificity for HDL3 devoid E apolipoprotein. was richest source protein. Both bound A-I A-II apolipoproteins retained activity after final purification. HB1 activity, not that HB2, lost treatment beta-mercaptoethanol, reduction did change molecular mass either Antibodies against or HB2 cross-react, preliminary structural investigations provide evidence to suggest are structurally related. We thus at least plasma-membrane bind HDL apolipoproteins, suggesting protein-protein interaction participates some degree mechanism recognition by cells.