Research on the RNA polymerase which has an affinity for auxin-binding protein.

从分离的绿豆细胞核中溶解核蛋白，用单q柱分离。将α -amanitin敏感RNA聚合酶活性的部分汇集到生长素结合蛋白- i （ABP-I）结合的Sepharose 4B柱上。RNA聚合酶活性完全保留在柱上，用0.3 M (NH_4)@>D22@>D2SO_4洗脱。采用Burgess等人的方法从小麦胚芽中纯化出RNA聚合酶II，并检测了其与ABP-I的相互作用。纯化的TNA聚合酶II保留在abp - i结合的Sepharose 4B亲和柱上，用0.3 M (NH_4)_2SO_4洗脱。根据这些结果，我们认为RNA聚合酶II与ABP-I具有亲和力，并且这种相互作用可能在基因表达中起作用。

Nucleoproteins were solubilized from isolated mung bean nuclei and separated by a column of mono Q. Fractions of alpha-amanitin-sensitive RNA polymerase activity were pooled and applied to a column of auxin-binding protein-I(ABP-I)-bound Sepharose 4B. RNA polymerase activity was completely retained on the column and eluted by 0.3 M (NH_4)@>D22@>D2SO_4.RNA polymerase II was purified from wheat germ by the method of Burgess et al. and examined an interaction for ABP-I. The purified TNA polymerase II was retained on the affinity column of ABP-I-bound Sepharose 4B and eluted by 0.3 M (NH_4)_2SO_4.From these results, we consider that RNA polymerase II have an affinity for ABP-I and the interaction may play a role for gene expression.