Lai P C, Peters E H, Lorscheider F L
Biochim Biophys Acta. 1978 Jul 21;535(1):138-49. doi: 10.1016/0005-2795(78)90040-5.
Bovine alpha1-fetoprotein was isolated from fetal calf serum by successive procedures of concanavalin A-Sepharose chromatography, DEAE-Sephadex chromatography, SP-Sephadex chromatography and preparative disc polyacrylamide gel electrophoresis. The bovine alpha1-fetoprotein preparation was considered homogeneous by several physicochemical and immunochemical criteria. Bovine alpha1-fetoprotein has a molecular weight of 68 000 with an amino acid composiotn similar to that of other mammalian alhpa1-fetoprotein. In addition, bovine alpha1-fetoprotein was shown to exist as two distinct variants on the basis of carbohydrate heterogeneity. alpha2-Fetoprotein and a new beta-fetoprotein were immunologically identified in fetal calf serum. These fetoproteins, like alpha1-fetoprotein, were not detectable in non-pregnant cow serum by immunoelectrophoresis.
通过伴刀豆球蛋白A-琼脂糖凝胶层析、二乙氨基乙基葡聚糖凝胶层析、磺丙基葡聚糖凝胶层析及制备性圆盘聚丙烯酰胺凝胶电泳等连续步骤，从胎牛血清中分离出牛α1-甲胎蛋白。根据多种物理化学和免疫化学标准，该牛α1-甲胎蛋白制剂被认为是均一的。牛α1-甲胎蛋白的分子量为68000，其氨基酸组成与其他哺乳动物的α1-甲胎蛋白相似。此外，基于碳水化合物的异质性，牛α1-甲胎蛋白显示为两种不同的变体。在胎牛血清中通过免疫鉴定出了α2-甲胎蛋白和一种新的β-甲胎蛋白。通过免疫电泳在未怀孕母牛血清中未检测到这些甲胎蛋白，如同未检测到α1-甲胎蛋白一样。
