Solvejg V. Reeh

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The amount of 140 individual proteins of E. coli B/r was measured during balanced growth in five different media. The abundance of each protein was determined from its absolute amount in 14C-glucose-minimal medium and a measurement of its relative amount at each growth rate using a double labeling technique. Separation of the proteins was carried out by(More)
Fed-batch production of recombinant beta-galactosidase in E. coli was studied with respect to the specific growth rate at induction. The cultivations were designed to induce protein production by IPTG at a glucose feed rate corresponding to high mu = 0.5 h(-1)) or low (mu = 0.1 h(-1)) specific growth rate. Protein production rate was approximately 100%(More)
Polypeptide chains of 10 aminoacyl-transfer ribonucleic acid synthetases (those for arginine, glutamine, glutamic acid, glycine, isoleucine, leucine, lysine, phenylalanine, threonine, and valine) have been identified in lysates of Escherichia coli resolved by the O'Farrell two-dimensional gel system. By labeling cells uniformly with [14C]glucose and by(More)
A specialized transducing bacteriophage lambdadpolCdap D-9 has been isolated that carries the structural gene for EF-Ts1 (tsf). The presence of EF-Ts among the proteins synthesized under the direction of this phage in UVL-inactivated cells has been detected by two-dimensional gel electrophoresis and has been verified by antibody precipitation. In an induced(More)
Transcriptional termination factor rho, the alpha subunit of RNA polymerase (RNA nucleotidyltransferase nucleosidetriphosphate: RNA nucleotidyltransferase, EC, and ribosomal protein S6 were resolved from whole-cell extracts of E. coli B/r by a high-resolution, two-dimensional polyacrylamide gel electrophoretic technique, and were identified through(More)
A previously isolated mutant of E. coli K12 HAK 88 [Kuwano, M., Endo, h & yamamoto, M. (1972) J. Bacteriol, 112, 1150-1156], contains a new protein that in two-dimensional gel electropherorgrams has the same molecular weight as normal elongation factor Tu, but whose isoelectric point is altered approximately 0.1 pH unit in the acidic direction. Peptide(More)
Analysis of the synthetic rate of individual protein species at various times after complete inhibition of transcription with either streptolygidin or rifampicin was carried out by two-dimensional polyacrylamide electrophoresis of total Escherichia coli cell extracts. The decay rate of the potential to synthesize different proteins was assumed to be equal(More)
An isogenic pair of Escherichia coli mutants (relA + tufB valS ts and relA1 tufB valS ts) has been cultured at several temperatures to establish various degrees of limitation for valyl-tRNA synthetase. The biosynthetic rate of 16 identifiable proteins, most of which are components of the transcription and translation apparatus, was measured by(More)
Escherichia coli has multiple forms of ribosomal protein S6, differing in number of glutamyl residues at the C-terminal end. Three forms are revealed when crude cell extracts are fractionated by a two-dimensional gel electrophoresis technique. Pulse-chase experiments show that the shortes and most alkaline form of S6 is the first to appear. In about one(More)
The steady-state levels of a number of aminoacyl-transfer ribonucleic acid synthetases are known to be positively correlated with growth rate in Escherichia coli. To describe the regulation of these enzymes during a nutritional shift-up, use was made of the recent identification of polypeptide chains of several synthetases in whole cell lysates resolved by(More)