Results 361 to 370 of about 1,293,873 (407)

Recombinant protein expression in Escherichia coli

Current Opinion in Biotechnology, 1999
Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics are far better characterized than those of any other microorganism. Recent progress in the fundamental understanding of transcription, translation, and protein folding in E.
openaire   +2 more sources

Hyperproduction of araC protein from Escherichia coli

Biochemistry, 1982
Hypersynthesis of araC protein from Escherichia coli has been accomplished. The araC gene was cloned on plasmid pBR322, and some of the noncoding DNA preceding the araC gene was removed by exonuclease digestion. Finally, a DNA fragment containing the lac promoter and ribosome binding site was placed in front the araC gene.
R F, Schleif, M A, Favreau
openaire   +2 more sources

DNA Replication Proteins of Escherichia Coli

Annual Review of Biochemistry, 1978
PERSPECTIVES AND SUMMARY ..... .. .. 1163 ESCHERICHIA COLI CHROMOSOME REPLICATION ........ .. ..... ...... .... 116S In Vivo DNA Replication 1165 In Vitro DNA Replication 1166 SINGLE-STRANDED CIRCULAR DNA-DEPENDENT DNA SYNTHESIS .... 1168 Priming of Single-Stranded DNA Synthesis ..
openaire   +2 more sources

Extracellular recombinant protein production from Escherichia coli

Biotechnology Letters, 2009
Escherichia coli is the most commonly used host for recombinant protein production and metabolic engineering. Extracellular production of enzymes and proteins is advantageous as it could greatly reduce the complexity of a bioprocess and improve product quality.
Ye, Ni, Rachel, Chen
openaire   +2 more sources

[Protein kinase activity in Escherichia coli].

Comptes rendus des seances de l'Academie des sciences. Serie D, Sciences naturelles, 1979
When growing E. coli in a minimal medium, at least four proteins from the soluble fraction and one ribosome-associated protein are found phosphorylated at the level of their threonine and serine residues.
Manai, M., Cozzone, A.
openaire   +2 more sources

Induction of protein X in Escherichia coli

Molecular and General Genetics MGG, 1977
Certain treatments that damage DNA and/or inhibit replication in E. coli have been reported to induce synthesis of a new protein, termed protein X, in recA+ lexA+ strains. We have examined some of the treatments that might induce protein X and we have, in particular, tested the hypothesis of Gudas and Pardee (1975) that DNA degradation products play an
J W, Little, P C, Hanawalt
openaire   +2 more sources

Strategies for protein coexpression in Escherichia coli

Nature Methods, 2006
E. coli is a convenient host for heterologous protein expression. Its advantages include high levels of heterologous gene expression and scalability of experiments, low cost, fast growth, a lack of posttranslational modification and an ability to express labeled (isotope or seleno-methionine) proteins.
Niraj H, Tolia, Leemor, Joshua-Tor
openaire   +2 more sources

Cysteinyl residues of Escherichia coli recA protein

Biochemistry, 1984
The Escherichia coli recA protein has three cysteinyl residues at positions 90, 116, and 129. All of them are reactive with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB). In the presence of ATP or ADP, only one cysteinyl residue reacts with DTNB. The residue was also reactive with N-[7-(dimethylamino)-4-methylcoumarinyl]maleimide (DACM) in the presence of
Seiki Kuramitsu, Kozo Hamaguchi, Hideki Tachibana, Toshihiro Horii, Kazuo Yoshimoto, Tomoko Ogawa, Hideyuki Ogawa   +6 more
openaire   +2 more sources

Penicillin-Binding Protein 5 of Escherichia coli

2013
Refereed/Peer ...
Malika Kumarasiri, Jed F. Fisher, Shahriar Mobashery   +2 more
openaire   +2 more sources

Protein translocation in Escherichia coli

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1994
R A, Arkowitz, M, Bassilana
openaire   +2 more sources