Rodokanaki A, Holmes R K, Borrás T
Laboratory of Mechanisms of Ocular Diseases, National Eye Institute, Bethesda, MD 20892.
Gene. 1989 May 30;78(2):215-24. doi: 10.1016/0378-1119(89)90224-2.
zeta-Crystallin is a major component of the water-soluble proteins of the guinea pig lens. We have constructed a lens cDNA library from one- to seven-day-old guinea pigs in the plasmid Bluescript KS+ and used the 16 amino acid (aa) sequence of a CNBr peptide to design an oligodeoxyribonucleotide probe. Analysis of two positive clones and direct sequence of the 5' end of the RNA resulted in the completion of a most probably full-length mRNA comprising 1842 nucleotides (nt). The ATG start codon occurs 83 nt downstream from the 5' end. The open reading frame, ending with a stop codon at nt position 1070, predicts a protein of 328 aa with a calculated Mr of 35,071. Comparison of the amino acid sequence with the National Biomedical Research Foundation protein data base reveals a significant similarity of zeta-crystallin with the enzyme of the alcohol dehydrogenase family.
ζ-晶体蛋白是豚鼠晶状体水溶性蛋白质的主要成分。我们用质粒pBluescript KS+构建了1至7日龄豚鼠晶状体的cDNA文库，并利用一个CNBr肽的16个氨基酸序列设计了一个寡脱氧核糖核苷酸探针。对两个阳性克隆的分析以及对RNA 5'端的直接测序，得到了一个最可能全长为1842个核苷酸（nt）的mRNA。ATG起始密码子位于5'端下游83 nt处。开放阅读框在nt位置1070处有一个终止密码子，预测有一个328个氨基酸的蛋白质，计算出的Mr为35,071。将氨基酸序列与国家生物医学研究基金会蛋白质数据库进行比较，发现ζ-晶体蛋白与醇脱氢酶家族的酶有显著相似性。
