A mutant rho ATPase from Escherichia col
โ
Kent, Rachel B. ;Guterman, Sonia K.
๐
Article
๐
1981
๐
Springer
๐
English
โ 566 KB
The Escherichia coli mutant rho-I15 suppresses lac operon polarity conferred by the lacZ: :IS1 insertion MS319. The ATPase activity of purified rho-115 protein was maximal at 40 ยฐ C, in contrast to 45 ยฐ C for rho +. At higher temperatures (50 ยฐ C, 55 ยฐ C), the fractions of activities at maximal temp