Vayda M E, Flint S J
J Virol. 1987 Oct;61(10):3335-9. doi: 10.1128/JVI.61.10.3335-3339.1987.
Digestion of adenovirus type 2 (Ad2) or Ad5 cores with micrococcal nuclease generated four nucleoprotein species that could be resolved by electrophoresis in low-ionic-strength polyacrylamide gels: these nucleoproteins displayed mobilities equivalent to those of DNA fragments of 900 to 1,025, 775 to 850, 650 to 725, and 525 to 600 base pairs (bp) and thus were readily distinguishable from HeLa cell mononucleosomes. The DNA fragments associated with the core nucleoprotein species were more than 250 to 90 bp long. Nucleoproteins containing 150, 120, or 90 bp of DNA were the most stable. Polypeptide VII was associated with each of the nucleoprotein species liberated from Ad2 cores. These data suggest that polypeptide VII and viral DNA of 90 to 150 bp comprise the unit particle of the Ad2 or Ad5 core nucleoproteins.
用微球菌核酸酶消化2型腺病毒(Ad2)或5型腺病毒(Ad5)核心产生了四种核蛋白种类,它们可通过在低离子强度聚丙烯酰胺凝胶中电泳进行分离:这些核蛋白的迁移率与900至1025、775至850、650至725和525至600碱基对(bp)的DNA片段相当,因此很容易与HeLa细胞单核小体区分开来。与核心核蛋白种类相关的DNA片段长度超过250至90 bp。含有150、120或90 bp DNA的核蛋白最稳定。多肽VII与从Ad2核心释放的每种核蛋白种类相关。这些数据表明,多肽VII和90至150 bp的病毒DNA构成了Ad2或Ad5核心核蛋白的单位颗粒。