Gorin M B, Cooper D L, Eiferman F, van de Rijn P, Tilghman S M
J Biol Chem. 1981 Feb 25;256(4):1954-9.
The amino acid sequence of mouse alpha-fetoprotein has been deduced from the nucleotide sequence of its mRNA and three chimeric plasmids containing overlapping segments of its cDNA. A comparison of the amino acid sequence with that of either human and bovine albumin reveals in each case a 32% conservation of primary sequence. In addition, using the regularly spaced positions of cystine bridges, a 2-dimensional structure was generated, which revealed the presence of 3 closely related domains within alpha-fetoprotein. The structures of these domains are identical with the triplicated domains previously observed in several mammalian albumins. These homologies lend strong circumstantial evidence to the proposal that these two proteins arose in evolution as the consequence of a duplication in a common tripartite ancestral gene.
小鼠甲胎蛋白的氨基酸序列已从其mRNA的核苷酸序列以及三个含有其cDNA重叠片段的嵌合质粒推导得出。将该氨基酸序列与人及牛白蛋白的氨基酸序列进行比较,结果显示在每种情况下一级序列的保守率均为32%。此外,利用胱氨酸桥的规则间隔位置构建了一个二维结构,该结构揭示了甲胎蛋白中存在3个紧密相关的结构域。这些结构域的结构与先前在几种哺乳动物白蛋白中观察到的三重结构域相同。这些同源性为以下提议提供了有力的间接证据:这两种蛋白质在进化过程中是由一个共同的三联祖先基因复制产生的。