Isolation of a second rifamycin-binding from Escherichia coli by affinity chromatography

Eur J Biochem. 1981 Jun;117(1):87-91. doi: 10.1111/j.1432-1033.1981.tb06306.x.

Abstract

When extracts of Escherichia coli are filtered through a Sepharose column containing covalently bound rifamycin a protein is bound which can be eluted either with a high concentration of urea or more specifically with low concentrations of rifamycins. Its Mr is 18,000 +/- 1,000 in the presence of dodecylsulfate, in its absence 36,000 +/- 3,000. The association constant of the protein for rifampicin is 2.4 +/- 0.5 x 10(-4) M with two binding sites per dimer as determined by equilibrium dialysis. Large amounts of this protein are released from the cells by an osmotic shock.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Chromatography, Affinity
  • Escherichia coli / metabolism*
  • Kinetics
  • Molecular Weight
  • Rifamycins / metabolism*

Substances

  • Rifamycins