Brock H W, Roberts D B
Eur J Biochem. 1980 May;106(1):129-35. doi: 10.1111/j.1432-1033.1980.tb06003.x.
Immunological data, amino acid composition, and coordinate control during development suggest that the alpha, beta and gamma subunits of the major protein of Drosophila larval serum (LSP-1) are coded for by genes which evolved by replications of an ancestral gene followed by mutation. In order to test this hypothesis, and to study the relationship of these genes with that coding for the second major larval serum protein subunits. One-dimensional maps generated by three different proteases showed many similarities among these proteins. Two-dimensional peptide mapping of the methionine-containing tryptic peptides showed that half of these peptides are common to all four larval serum protein subunits, and that about two-thirds are common to the three LSP-1 subunits. These observations show that the LSP-1 subunits are more closely related to each other than any is to LSP-2, and supported the initial suggestion that the proteins are homologous. Because the genes for the LSP-1 subunits are each located on a different chromosome, the LSP-1 subunits are a suitable system for investigating the evolution and dispersal of related genes, and trans control in eukaryotes.
免疫学数据、氨基酸组成以及发育过程中的协同调控表明，果蝇幼虫血清主要蛋白质（LSP-1）的α、β和γ亚基由通过祖先基因复制后发生突变而进化的基因编码。为了验证这一假设，并研究这些基因与编码第二种主要幼虫血清蛋白质亚基的基因之间的关系。由三种不同蛋白酶生成的一维图谱显示这些蛋白质之间有许多相似之处。含甲硫氨酸的胰蛋白酶肽的二维肽图谱表明，这些肽中有一半是所有四种幼虫血清蛋白质亚基共有的，并且约三分之二是三种LSP-1亚基共有的。这些观察结果表明，LSP-1亚基彼此之间的关系比它们与LSP-2的关系更为密切，并支持了这些蛋白质是同源的最初推测。由于LSP-1亚基的基因分别位于不同的染色体上，LSP-1亚基是研究相关基因的进化和分散以及真核生物中的反式调控的合适系统。
