Schonfeld G, Frick M S, Bailey A P
J Lipid Res. 1976 Jan;17(1):25-9.
A double antibody radioimmunoassay (RIA) for rat apolipoprotein A-I is reported. The ApoA-I isolated from delipidated HDL by gel filtration yielded a single band on polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS), and its amino acid composition resembled that reported by others. ApoA-I was iodinated by lactoperoxidase and the resulting 125I-apoA-I was purified by gel filtration. Up to 93% of 125I-apoA-I was precipitable by antibody and greater than 99% of bound 125I-apoA-I was displaced by "cold" apoA-I. Other rat lopoproteins and apolipoproteins did not react in this system. Human plasma were also not reactive, nor were dog, goat, and sheep plasmas.
本文报道了一种用于大鼠载脂蛋白A-I的双抗体放射免疫分析方法（RIA）。通过凝胶过滤从脱脂高密度脂蛋白中分离得到的载脂蛋白A-I在十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶电泳上呈现单一谱带，其氨基酸组成与其他文献报道的相似。载脂蛋白A-I经乳过氧化物酶碘化，所得的125I-载脂蛋白A-I通过凝胶过滤进行纯化。高达93%的125I-载脂蛋白A-I可被抗体沉淀，且超过99%结合的125I-载脂蛋白A-I可被“冷”载脂蛋白A-I置换。其他大鼠脂蛋白和载脂蛋白在该系统中无反应。人血浆也无反应，狗、山羊和绵羊血浆同样如此。
