@article {Yang:August 1997:1046-5928:320,
	author = "Yang Q.H.",
	author = "Wu C.L.",
	author = "Lin K.",
	author = "Li L.",
	title = "Low Concentration of Inducer Favors Production of Active Form of 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase in Escherichia coli",
	journal = "Protein Expression and Purification",
	volume = "10",
	year = "August 1997",
	abstract = "<P> Expression of chicken and rat liver bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, in Escherichia coli encountered two common problems: the chicken enzyme was liable to proteolysis and the rat enzyme was prone to form inclusion bodies. Reducing the rate of protein synthesis by lowering either growth temperature or isopropyl-beta- d -thiogalactopyranoside (IPTG) concentration alleviated these two problems. Growth at 22#&176;C was optimum for expression of both enzymes. The optimum range of IPTG concentration for expression was 0.1-1 mu m for the chicken liver bifunctional enzyme and 10 mu m for rat liver enzyme. The components of growth medium also influenced the production. Compared with Luria-Bertani medium, an enriched medium-tryptone-phosphate medium-tripled the production of the active enzymes. Addition of glucose (0.2%) doubled the expression level of active chicken liver enzyme, but reduced the production of active rat liver enzyme to half the maximal level, while the phosphate in tryptone-phosphate medium had no effect on the production of the two enzymes.</P>",
	pages = "320-324(5)",
	url = "http://www.ingentaconnect.com/content/ap/pt/1997/00000010/00000003/art00749"
}