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Enzymatic extraction of purified low density lipoprotein (LDL) from rabbit or bovine serum results in fragmentation and solubilization of the material. This extract (LDL proteose) contains activities that are either specific or more likely nonspecific activities of cellular protein, because: 1. In vitro additions of purified apolipoprotein (apo) B and apoA-I, but not of purified apoE, to LDL proteose result in the formation of low density lipoprotein-like particles in tissue culture. 2. In the presence of purified apoB, a preparation of rat fibroblasts binds LDL proteose, and, like purified apoB, transfers LDL proteose from cells to purified rat hepatic receptors. 3. Washing serum-starved rat fibroblasts with LDL proteose results in a significant enrichment of their cell surface receptors to about 30% of the total number of receptors in the cells. 4. Rat hepatic receptors retain 50% of their activity after incubation with 50 micrograms of LDL proteose for 2 h, whereas 50 micrograms of purified apoB transfer 50% of the activity of the receptors to LDL. 5. Hepatic receptors decrease in density during in vivo transport of LDL. 6. A partially purified preparation of aortic receptor has a Stokes radius of 105 A and a sedimentation coefficient of 5.3 S.Q:
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