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用酶免疫测定、配体印迹、酶水解、化学修饰等方法研究ｒＨＢｓＡｇ结合ａｐｏＨ的机理。实验结果表明，ｒＨＢｓＡｇ结合ａｐｏＨ是不依赖于Ｃａ＋＋、Ｍｇ＋＋等二价阳离子的，其最适ｐＨ在６．５～８．０。切除ａｐｏＨ上的神经氨酸和Ｎ－糖苷键，ａｐｏＨ结合力无变化，说明糖基不是ａｐｏＨ结合ｒＨＢｓＡｇ所必需的。化学修饰ａｐｏＨ的精氨酸残基对ａｐｏＨ的结合力无影响。然而，修饰其中几个赖氨酸残基即可减弱直至完全破坏ａｐｏＨ的结合力，说明赖氨酸残基与ａｐｏＨ结合ｒＨＢｓＡｇ有关。由于ａｐｏＨ与脂蛋白，特别是ＣＭ和ＨＤＬ结合，ＨＢＶ有可能通过ａｐｏＨ，结合ＣＭ、ＨＤＬ等，在脂蛋白代谢过程中进入肝细胞。
The mechanism of rHBsAg binding to apoH was studied by enzyme immunoassay, ligand blot, enzymatic hydrolysis and chemical modification. The experimental results show that rHBsAg binding apoH is not dependent on the divalent cations such as Ca ++, Mg ++, and the optimum pH is between 6.5 and 8.0. Excision of apoH by neuraminic acid and N-glycosidic bonds showed no change in apoH binding, indicating that glycosylation is not required for apoH binding to rHBsAg. Arginine residues in chemically modified apoH had no effect on the binding of apoH. However, modification of several of these lysine residues attenuated the binding until a complete destruction of apoH, suggesting that lysine residues are associated with apoH binding to rHBsAg. Since apoH binds to lipoproteins, especially CM and HDL, it is possible for HBV to enter hepatocytes during the metabolism of lipoproteins via apoH, CM, HDL, and the like.