Goodall G J, Dominguez F, Horecker B L
Proc Natl Acad Sci U S A. 1986 Dec;83(23):8926-8. doi: 10.1073/pnas.83.23.8926.
A cDNA library was constructed from human spleen mRNA and screened for clones containing cDNAs coding for prothymosin alpha. A clone containing a 503-base-pair insert including the entire coding sequence for the translated portion of the mRNA was isolated. The deduced amino acid sequence confirms and completes the partial sequence of human prothymosin alpha determined by protein sequencing methods. The presence of an initiator codon immediately preceding the codon for the NH2-terminal serine residue and of a terminator codon immediately following the codon for Asp-109, the COOH-terminal residue, suggests that prothymosin alpha is synthesized without formation of a larger precursor polypeptide. Analysis of the 5' sequence preceding the initiator methionine codon excluded the presence of a signal peptide in the translated sequence.
从人脾脏mRNA构建了一个cDNA文库，并筛选含有编码前胸腺素α的cDNA的克隆。分离出一个含有503个碱基对插入片段的克隆，该插入片段包括mRNA翻译部分的完整编码序列。推导的氨基酸序列证实并完善了通过蛋白质测序方法确定的人前胸腺素α的部分序列。在NH2-末端丝氨酸残基的密码子之前紧邻一个起始密码子，在COOH-末端残基Asp-109的密码子之后紧邻一个终止密码子，这表明前胸腺素α是在不形成更大前体多肽的情况下合成的。对起始甲硫氨酸密码子之前的5'序列分析排除了翻译序列中信号肽的存在。
