id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-007279-ewcgkx0h	Song, Jong-Am	Human G-CSF synthesis using stress-responsive bacterial proteins	2009-07-01		.txt	text/plain	3381	159	44	We previously reported that under the stress condition caused by the addition of 2-hydroxyethyl disulfide, a thiol-specific oxidant, to growing cultures of Escherichia coli BL21(DE3), a population of stress-responsive proteins [peptidyl-prolyl cis–trans isomerase B (PpiB), bacterioferritin (Bfr), putative HTH-type transcriptional regulator yjdC (YjdC), dihydrofolate reductase (FolA), chemotaxis protein cheZ (CheZ), and glutathione synthetase (GshB)] were significantly upregulated when compared with the nonstress condition. When those stress-responsive proteins were used as fusion partners for the expression of human granulocyte colony-stimulating factor (hG-CSF), the solubility of hG-CSF was dramatically enhanced in E. We found that these relatively small stress-responsive proteins were highly effective in enhancing the solubility of recombinant hG-CSF when used as fusion partner, which will be discussed next. coli cytoplasm dramatically increased when the stress-responsive proteins were used as fusion partners, indicating that the fusion expression partners were highly effective solubility enhancers. Solubility enhancement of aggregation-prone heterologous proteins by fusion expression using stress-responsive Escherichia coli protein	./cache/cord-007279-ewcgkx0h.txt	./txt/cord-007279-ewcgkx0h.txt