Strain G C, Mullinix K P, Bogorad L
Proc Natl Acad Sci U S A. 1971 Nov;68(11):2647-51. doi: 10.1073/pnas.68.11.2647.
Two DNA-dependent RNA polymerases of nuclear origin have been purified from leaves of Zea mays. The two enzymes can be separated on DEAE-cellulose columns. Enzymes I and II are eluted with 0.08 and 0.20 M (NH(4))(2)SO(4), respectively. Both enzymes prefer maize nuclear DNA as a template; they are also more active in the presence of Mg(++) than Mn(++) and are inhibited by (NH(4))(2)-SO(4) or KCl. Neither enzyme is inhibited by rifamycin SV. Enzyme II is strongly inhibited by alpha-amanitin, whereas enzyme I is not significantly affected. Their ability to use native and denatured DNA as templates varies according to the extent and method of purification of the polymerase. Furthermore, enzyme II can be resolved by DEAE-chromatography or glycerol-gradient centrifugation into two components, one of which prefers native DNA, while the other prefers denatured DNA.
已从玉米叶片中纯化出两种核源的依赖DNA的RNA聚合酶。这两种酶可在DEAE - 纤维素柱上分离。酶I和酶II分别用0.08和0.20 M硫酸铵洗脱。两种酶都更倾向于以玉米核DNA作为模板；它们在镁离子存在下比在锰离子存在下更具活性，并且会受到硫酸铵或氯化钾的抑制。两种酶均不受利福霉素SV的抑制。酶II受到α - 鹅膏蕈碱的强烈抑制，而酶I则未受到显著影响。它们使用天然DNA和变性DNA作为模板的能力会根据聚合酶的纯化程度和方法而有所不同。此外，酶II可通过DEAE - 色谱法或甘油梯度离心法解析为两个组分，其中一个组分更倾向于天然DNA，而另一个则更倾向于变性DNA。
