Abstract
In the present work, an apoprotein solution was prepared from hen’s egg yolk low density lipoprotein (LDL) without using detergents; LDL was delipidated with chloroform-methanol (2:1) and solubilized by sonication with 80% ethylene glycol. An apoLDl-phospholipid complex was prepared by sonicating this apoprotein solution with an egg yolk lecithin suspension. Although high-molecular-weight polypeptides of apoLDL formed an insoluble complex with lecithin, its low- molecular-weight polypeptides formed a soluble complex. The soluble apoLDl-phospholipid complex gave only one peak on gel filtration on Sephacryl S-400.Emulsifying properties of the soluble apoLDl-phospholipid complex were much better than those of either lecithin vesicles or lecithin suspensions with the same concentration of phospholipid, and almost the same as those of LDL. These results seem to show that the superior emulsifying properties of LDL depend on the characteristic structure of its lipid-protein complexes.
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