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Purification and properties of phage P22 c2 repressor.

作者信息

Ballivet M, Eisen H

出版信息

Eur J Biochem. 1978 Jan 2;82(1):175-80. doi: 10.1111/j.1432-1033.1978.tb12009.x.

Abstract

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.

摘要

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