@misc{Szczepanek_Andrzej_Methods_1994,
 author={Szczepanek, Andrzej and Płucienniczak, Andrzej},
 volume={27},
 number={4},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.27, 4 (1994)-.},
 howpublished={online},
 year={1994},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 abstract={Escherichia coli is the most useful bacterial species applied to genetic engineering in recombinant proteins production process. The supply of many polipeptides whith potential clinical orindustrial use is often limited by their low natural availability. Overexpressed polipeptides mayeither be located in the cytoplasm and periplasm of E. coli or secreted through the cell membraneinto the growth medium. Foreign proteins can be expressed in E. coli cells directly or as fusionproteins with prokaryotic sequences. Frequently, the overexpressed proteins acumulate in thebacterial cytoplasm or periplasm in the form of insoluble inclusion bodies.This review considers isolation, purification, solubilization and renaturation of recombinantproteins from E. coli cells, whieh is still a serious methodological and technical problem.},
 title={Methods for isolation, purification and renaturation of recombinant proteins obtained in Escherichia coli bacteria},
 type={Text},
 URL={http://www.rcin.org.pl/Content/148136/PDF/POZN271_183649_biotechnologia-1994-no4-szczepanek.pdf},
 keywords={biotechnology},
}