Purification and properties of phage P22 c2 repressor.
Purification and properties of phage P22 c2 repressor.
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噬菌体 P22 c2 阻遏蛋白的纯化和特性。
DOI：
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发表时间：
1978
期刊：
影响因子：
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通讯作者：
H. Eisen
中科院分区：
文献类型：
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作者：
M. Ballivet;H. Eisen
噬菌体P22的c2抑制子已纯化为均一。它与lambdaimm21和P22 DNA特异性结合。它与假定的操作员突变体P22 VIRB的亲和力降低。在0℃、20℃和32℃时，c2阻遏物与lambdaimm21DNA形成的复合体的初始解离速率分别为0.02min-1、0.08min-1和0.17min-1。测定了c2阻遏物与Lambdaimm21操纵子OR、OL和OR Vira形成的复合体的解离速率，并与21Ci阻遏物的相应解离速率进行了比较。
The c2 repressor of phage P22 has been purified to homogeneity. It specifically binds to lambdaimm21 and P22 DNA. Its affinity for the presumed operator mutant P22 virB is reduced. The initial dissociation rates of the complex between c2 repressor and lambdaimm21 DNA are 0.02 min-1 at 0 degrees C, 0.08 min-1 at 20 degrees C and 0.17 min-1 at 32 degrees C. The dissociation rates of complexes formed between the c2 repressor and the lambdaimm21 operators OR, OL and OR vira were measured and compared to the corresponding rates obtained with 21 cI repressor.