Stability of Escherichia coli Membrane Proteins During Chloramphenicol Treatment

Stability of Escherichia coli membrane proteins during chloramphenicol treatment.

It is shown that there is no degradation of previously formed inner and outer membrane proteins of Escherichia coli during 1 h of chloramphenicol treatment.

Stability of Recombinant Proteins in Escherichia coli: The Effect of Co-Expression of Five Different Chaperone Sets

Chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. Over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell. On the basis of this hypothesis, five different plasmids with 5 different combinations of 6 chaperones molecule, transformed into Escherichia coli along with human basic Fibroblast Grow...

A Chimeric Vaccine Consisting of Highly Immunogenic Regions form Escherichia coli Iron Regulated Outer-Membrane Proteins: An In Silico Approach

Lysyl-derived aldehydes in outer membrane proteins of Escherichia coli.

The major outer membrane proteins from Escherichia coli K-12 are modified to contain alpha-aminoadipic acid delta-semialdehyde (allysine). The allysine was found to be derived from lysine and it was identified by derivatizing it to chloronorleucine by reduction, alpha-aminoadipic acid by oxidation, and to alpha,epsilon-diaminopimelic acid by reacting it with CN- and NH3. The alpha-aminoadipic a...

Cloning of Bordetella pertussis outer membrane proteins in Escherichia coli.

We constructed and screened a gene bank of phase I chromosomal DNA of Bordetella pertussis in Escherichia coli. A single immunopositive clone was recovered, and the hybrid plasmid obtained, designated pFSH200, had a molecular size of 46.6 kilobases. Smaller derivatives were generated by partial digestion of plasmid pFSH200 and were further characterized. One such derivative, plasmid pFSH201, co...