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首页> 外文期刊>Journal of Virology >Adenovirus type 2 terminal protein: purification and comparison of tryptic peptides with known adenovirus-coded proteins.
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Adenovirus type 2 terminal protein: purification and comparison of tryptic peptides with known adenovirus-coded proteins.

机译：腺病毒2型末端蛋白质：纯化和患有已知腺病毒编码蛋白的胰蛋白病毒肽的比较。

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摘要

The protein covalently bound to the 5' termini of adenovirus type 2 DNA has been purified from virus labeled with [35S]methionine, using exclusion chromatography of disrupted virions to isolate the DNA-protein complex, which is then digested with DNase. The terminal protein isolated from mature virus is most effectively labeled if the cells are exposed to [35S]methionine during the "intermediate" period of 13 to 21 h postinfection, suggesting that the protein is synthesized during this interval. The tryptic peptides of the terminal protein were compared with those of several known adenovirus-coded proteins and found to be unrelated. In particular, the terminal protein is not related to the 38-50K early proteins encoded by the leftmost 4.4% of the adenovirus genome, one region essential for the transforming activity of the virus. Neither is it related to the 72K single-strand-specific DNA binding protein, the minor virion component IVa2, or the major capsid component hexon.
机译：通过破坏的病毒粒子标记的病毒纯化与腺病毒2型DNA的5'末端的蛋白质共价结合的腺病毒2 DNA的蛋白质从标记的病毒中纯化，以分离DNA蛋白质复合物，然后用DNase消化。从成熟病毒中分离的末端蛋白最有效地标记，如果细胞在“中间体”期间在13至21小时的染色期间暴露于[35s]甲硫氨酸，这表明在该间隔期间合成蛋白质。将终蛋白的胰蛋白酶肽与几种已知的腺病毒编码蛋白的蛋白质进行比较，发现不相关。特别地，终端蛋白质与由腺病毒基因组的最左边的4.4％编码的38-50k早期蛋白质无关，对于转化病毒的转化活性至关重要的一个区域。它既不是与72K单链特异性DNA结合蛋白，次要病毒酮组分IVA2或主要衣壳组分己零的相关。

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