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正常极低密度脂蛋白(n-VLDL)经胰蛋白酶降解后，载脂蛋白(Apo)E在电泳图谱上消失，ApoB-100水解成数个分子量小于10万的片段。酶解的n-VLDL仍可竞争性抑制小鼠腹腔巨噬细胞(MPM)结合、摄取与降解（125）~I-n-VLDL，且与n-VLDL同等有效。抗ApoB-100单抗有抑制（125）~I-n-VLDL与MPM的相互作用。结果表明ApoB-100在VLDL受体摄取n-VLDL的过程中起着配体的作用。
After normal very-low density lipoprotein (n-VLDL) is degraded by trypsin, apolipoprotein (Apo) E disappears on the electrophoretogram and ApoB-100 is hydrolyzed into several fragments with molecular weight less than 100,000. Enzymatically hydrolyzed n-VLDL can competitively inhibit mouse peritoneal macrophage (MPM) binding, uptake and degradation (125) ~ I-n-VLDL, and is as effective as n-VLDL. Anti-ApoB-100 mAb inhibits the interaction of (125) ~ I-n-VLDL with MPM. The results show that ApoB-100 plays a ligand role in the uptake of n-VLDL by VLDL receptors.