Formation of Soluble Recombinant Proteins in Escherichia Coli is Favored by Lower Growth Temperature
- 1 March 1988
- journal article
- Published by Springer Nature in Nature Biotechnology
- Vol. 6 (3) , 291-294
- https://doi.org/10.1038/nbt0388-291
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Mx protein: Constitutive expression in 3T3 cells transformed with cloned Mx cDNA confers selective resistance to influenza virusCell, 1986
- Isolation and Purification of Protein Granules from Escherichia coli Cells Overproducing Bovine Growth HormoneBio/Technology, 1985
- Site-specific mutagenesis of the human fibroblast interferon gene.Proceedings of the National Academy of Sciences, 1984
- Roles of the 29-138 disulfide bond of subtype A of human .alpha. interferon in its antiviral activity and conformational stabilityBiochemistry, 1984
- Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerasePublished by Elsevier ,1984
- Cytoplasmic Inclusion Bodies in Escherichia coli Producing Biosynthetic Human Insulin ProteinsScience, 1982
- Expression of human immune interferon cDNA in E. coli and monkey cellsNature, 1982
- Structure and function of Escherichia coli ribosomes: VI. Mechanism of assembly of 30 s ribosomes studied in vitroJournal of Molecular Biology, 1969
- On the Stabilization of Ribonuclease S-Protein by Ribonuclease S-PeptideJournal of Biological Chemistry, 1969
- Microheterogeneity of plasma albumins. V. Permutations in disulfide pairings as a probable source of microheterogeneity in bovine albuminBiochemistry, 1969