Purification and Properties of Phage P22 c2 Repressor
Open Access
- 1 January 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 82 (1), 175-180
- https://doi.org/10.1111/j.1432-1033.1978.tb12009.x
Abstract
The c2 repressor of phage P22 was purified to homogeneity. It specifically binds to [phage] .lambda.imm21 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 .lambda.imm21 DNA are 0.02 min-1 at 0.degree. C, 0.08 min-1 at 20.degree. C and 0.17 min-1 at 32.degree. C. The dissociation rates of complexes formed between the c2 repressor and the .lambda.imm21 operators OR, OL and OR vira were measured and compared to the corresponding rates obtained with 21 cI repressor.This publication has 14 references indexed in Scilit:
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