Kerckaert J P, Bayard B, Biserte G
Biochim Biophys Acta. 1979 Jan 25;576(1):99-108. doi: 10.1016/0005-2795(79)90488-4.
Polyacrylamide gel electrophoresis and crossed immuno-affino-electrophoresis with several free lectins have been used to characterize and to compare the molecular heterogeneity of rat, mouse and human alpha1-fetoproteins. Each alpha1-fetoprotein contains a variable number of electrophoretic variants depending on the gel porosity. In SDS electrophoresis, two molecular size populations are present in rat alpha1-fetoprotein (Mr = 74 000 and 72 000) and in mouse alpha1-fetoprotein (Mr = 73 000 and 72 000) but only one is observed in human alpha1-fetoprotein (Mr = 70 000). The crossed immuno-affino-electrophoresis patterns square with affinity chromatography results and reveal a marked and characteristic heterogeneity for the three alpha1-fetoprotein species with Concanavalin A, Ricinus communis and Lens culinaris lectins. No lectin-alpha-fetoprotein interaction is apparent with Ulex, Lotus and wheat germ lectins. Since similar patterns are obtained whether with purified alpha1-fetoprotein or with unfractionated fresh fetal sera, it is likely that this heterogeneity is not a consequence of artefactual molecular modifications arising during the purification procedure.
利用聚丙烯酰胺凝胶电泳以及与几种游离凝集素进行的交叉免疫亲和电泳，对大鼠、小鼠和人类甲胎蛋白的分子异质性进行了表征和比较。根据凝胶孔隙率的不同，每种甲胎蛋白都含有数量不等的电泳变体。在十二烷基硫酸钠电泳中，大鼠甲胎蛋白（分子量=74000和72000）和小鼠甲胎蛋白（分子量=73000和72000）呈现出两个分子大小群体，但人类甲胎蛋白（分子量=70000）仅观察到一个群体。交叉免疫亲和电泳图谱与亲和层析结果相符，并且显示出三种甲胎蛋白与伴刀豆球蛋白A、蓖麻凝集素和菜豆凝集素相互作用时具有明显且独特的异质性。与荆豆凝集素、百脉根凝集素和麦胚凝集素未观察到凝集素-甲胎蛋白相互作用。由于无论是使用纯化的甲胎蛋白还是未分级的新鲜胎血血清都能获得相似的图谱，因此这种异质性很可能不是纯化过程中人为分子修饰的结果。
