Law S W, Dugaiczyk A
Nature. 1981 May 21;291(5812):201-5. doi: 10.1038/291201a0.
The entire DNA complementary to murine alpha-fetoprotein mRNA has been cloned in the plasmid vector pBR322 and its complete nucleotide sequence determined. The deduced amino acid sequence identifies a hydrophobic prepeptide of 19 amino acids and the complete primary structure of alpha-fetoprotein. Its structure reveals extensive homology to serum albumin and suggests that there are 15 disulphide bridges in the alpha-fetoprotein molecule, all at the same positions as those found in albumin. The AFP molecule can be organized into a three-domain structure almost identical to that of serum albumin, suggesting a common ancestral origin of the two proteins.
与鼠α-甲胎蛋白mRNA互补的完整DNA已克隆到质粒载体pBR322中，并测定了其完整的核苷酸序列。推导的氨基酸序列确定了一个由19个氨基酸组成的疏水前肽以及α-甲胎蛋白的完整一级结构。其结构显示与血清白蛋白有广泛的同源性，并表明α-甲胎蛋白分子中有15个二硫键，所有这些二硫键都位于与白蛋白中发现的二硫键相同的位置。AFP分子可以组织成一个与血清白蛋白几乎相同的三结构域结构，这表明这两种蛋白质有共同的祖先起源。
