Kerckaert J P, Bayard B, Debray H, Sautière P, Biserte G
Biochim Biophys Acta. 1977 Aug 23;493(2):293-303. doi: 10.1016/0005-2795(77)90185-4.
Two electrophoretic forms of rat alpha-fetoprotein were purified using immunosorbent chromatography and preparative electrophoresis on polyacrylamide gel slabs. Some of their respective chemical properties and their affinity for the Ricinus communis lectin (RCAI) were compared. Electrophoresis on polyacrylamide gradient gel in the presence of sodium dodecyl sulfate indicated a slight difference in molecular 74 000 for the slow alpha-fetoprotein (AFPA) and 72000 for the fat alpha-fetoprotein (AFPB). no significant difference in amino acid composition between AFPA and AFPB was found. A residue of valine was identified at the C-germinal end of both alpha-fetoproteins. The analysis of the CNRr-cleavage products reveals slight differences between AFPS and AFPB. The slow moving alpha-fetoprotein could be further fractionated on RCAI-sepharose column in two components, AFPA1 and AFPA2 differing by their sialic acid content.
采用免疫吸附色谱法和聚丙烯酰胺凝胶板制备电泳法对大鼠甲胎蛋白的两种电泳形式进行了纯化。比较了它们各自的一些化学性质以及它们对蓖麻凝集素（RCAI）的亲和力。在十二烷基硫酸钠存在下进行聚丙烯酰胺梯度凝胶电泳，结果表明，慢泳动甲胎蛋白（AFPA）的分子量略有差异，为74000，快泳动甲胎蛋白（AFPB）的分子量为72000。未发现AFPA和AFPB在氨基酸组成上有显著差异。在两种甲胎蛋白的C末端均鉴定出缬氨酸残基。对CNRr裂解产物的分析表明，AFPS和AFPB之间存在细微差异。慢泳动甲胎蛋白在RCAI-琼脂糖柱上可进一步分离为两个组分，即AFPA1和AFPA2，它们的唾液酸含量不同。
