Al-Awqati M A, Gordon Y B, Chard T
Clin Chim Acta. 1978 Oct 16;89(2):173-82. doi: 10.1016/0009-8981(78)90316-9.
Highly purified human alphafetoprotein has been isolated from amniotic fluid and fetal livers by a combination of salting-out, and gel filtration, ion exchange, and concanavalin-A affinity chromatography. They yield ranged from 25 to 37%, and purity was demonstrated by radioimmunodiffusion, crossed radioimmunoelectrophoresis, polyacrylamide gel electrophoresis, and comparison with other preparations by radioimmunoassay. Immunochemical potency by weight of alphafetoprotein purified from amniotic fluid was similar to that from fetal liver, with molecular weights of 70 000 and 68 500 respectively. The amino acid and carbohydrate composition is also reported. This physicochemical method is relatively simple and inexpensive and is well suited for large scale production.
通过盐析、凝胶过滤、离子交换和伴刀豆球蛋白A亲和层析相结合的方法,已从羊水和胎儿肝脏中分离出高纯度的人甲胎蛋白。其产率在25%至37%之间,通过放射免疫扩散、交叉放射免疫电泳、聚丙烯酰胺凝胶电泳以及与其他制剂进行放射免疫测定比较来证明其纯度。从羊水中纯化的甲胎蛋白按重量计的免疫化学效力与从胎儿肝脏中纯化的相似,分子量分别为70000和68500。还报道了其氨基酸和碳水化合物组成。这种物理化学方法相对简单且成本低廉,非常适合大规模生产。