id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-253709-frauasts	Lan, Dongming	An improved nonchromatographic method for the purification of recombinant proteins using elastin-like polypeptide-tagged proteases	2011-08-15		.txt	text/plain	2063	112	52	title: An improved nonchromatographic method for the purification of recombinant proteins using elastin-like polypeptide-tagged proteases Abstract Proteins fused to the elastin-like polypeptide (ELP) tag can be selectively separated from crude cell extract without chromatography. Proteins fused to the elastin-like polypeptide (ELP) tag can be selectively separated from crude cell extract without chromatography. Among them, Meyer and Chilkoti reported a nonchromatographic method for purification of recombinant proteins using an elastin-like polypeptide (ELP) 2 tag [1] . This characteristic transition allows the recombinant ELP fusion protein to be isolated from the cell lysate by repeated steps of aggregation, centrifugation, and resolubilization without chromatography. Recombinant ELP fusion proteins at different expression levels can be efficiently recovered by the ITC method [4, 5] . ELP-3C protease was produced at a high level with an apparent molecular weight of approximately 58 kDa. To aggregate ELP-3C protease, solid NaCl was added into the cleared lysate to a final concentration of 2 M at room temperature to trigger the phase transition of ELP.	./cache/cord-253709-frauasts.txt	./txt/cord-253709-frauasts.txt