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Enhanced heterologous gene expression in novel rpoH mutants of Escherichia coli

Autor: M G Obukowicz, N R Staten, G G Krivi

Publikováno v: Applied and Environmental Microbiology. 58:1511-1523

Extragenic temperature-resistant suppressor mutants of an rpoD800 derivative of Escherichia coli W3110 were selected at 43.5 degrees C. Two of the mutants were shown to have a phenotype of enhanced accumulation of heterologous proteins. Genetic mappi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::336c0a393ac4c734c15cc4c87dbc6525
https://doi.org/10.1128/aem.58.5.1511-1523.1992

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Novel recombinant analogues of bovine placental lactogen. G133K and G133R provide a tool to understand the difference between the action of prolactin and growth hormone receptors

Autor: D, Helman, N R, Staten, J, Grosclaude, N, Daniel, C, Nespoulous, J, Djiane, A, Gertler

Publikováno v: The Journal of biological chemistry. 273(26)

Two new analogues of bovine placental lactogen (bPL), bPL(G133K) and bPL(G133R), were expressed in Escherichia coli, refolded, and purified to a native form. Binding experiments, which are likely to represent the binding to site 1 only, to intact FDC

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a9b17e7d796a954dfda1ba51a5f1e269
https://pubmed.ncbi.nlm.nih.gov/9632658

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Ligand-specific dimerization of the extracellular domain of the bovine growth hormone receptor

Autor: N R, Staten, J C, Byatt, G G, Krivi

Publikováno v: The Journal of biological chemistry. 268(25)

The bovine growth hormone (bGH) receptor and its extracellular domain (bGHBP) bind two protein hormones with high affinity; bGH and bovine placental lactogen (bPL). However, each of these hormones bind with a different stoichiometry. bGH binds to the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2802704960761015976f0fa95eab3525
https://pubmed.ncbi.nlm.nih.gov/8360148

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