Tikkanen M J, Cole T G, Hahm K S, Krul E S, Schonfeld G
Arteriosclerosis. 1984 Mar-Apr;4(2):138-46. doi: 10.1161/01.atv.4.2.138.
Epitope expression was studied in both denatured apolipoprotein B (apo B) on Western blots and in intact low density lipoprotein (LDL) and very low density lipoprotein subfractions VLDL1 (Sf120-400), VLDL2 (Sf60-120), and VLDL3 (Sf20-60) in competitive binding immunoassays with the aid of six monoclonal anti-LDL antibodies. The apo B in all lipoprotein fractions was shown to bind to all antibodies, but significant differences in apo B epitope expression were observed. On the average, the immunoreactivity of VLDL subfractions (expressed as binding affinity and as relative 125I-LDL displacing potency) decreased with increasing flotation rate. Similarly, VLDL1 was less immunoreactive than lipolyzed "remnants" of VLDL1 after treatment with bovine milk lipoprotein lipase. The results indicate that, even when lipoprotein fractions obtained from the same individual and having the same kind of apo B subspecies were compared, significant differences in immunoreactivity occurred due to the modulating effect of other lipoprotein components on apo B epitope expression.
利用六种抗低密度脂蛋白单克隆抗体，通过竞争性结合免疫测定法，在蛋白质印迹法中对变性载脂蛋白B（apo B）以及完整的低密度脂蛋白（LDL）和极低密度脂蛋白亚组分VLDL1（Sf120 - 400）、VLDL2（Sf60 - 120）和VLDL3（Sf20 - 60）中的表位表达进行了研究。结果表明，所有脂蛋白组分中的apo B均能与所有抗体结合，但在apo B表位表达上观察到显著差异。平均而言，极低密度脂蛋白亚组分的免疫反应性（以结合亲和力和相对125I - LDL置换能力表示）随漂浮率增加而降低。同样，在用牛乳脂蛋白脂肪酶处理后，VLDL1的免疫反应性低于VLDL1的脂解“残粒”。这些结果表明，即使比较来自同一个体且具有相同种类apo B亚型的脂蛋白组分，由于其他脂蛋白成分对apo B表位表达的调节作用，免疫反应性仍会出现显著差异。
