Methods for isolation, purification and renaturation of recombinant proteins obtained in Escherichia coli bacteria

• Authors: A. Szczepanek , A. Plucienniczak
• Languages of publication: PL

Abstracts

EN

Escherichia coli is the most useful bacterial species applied to genetic engineering in recombinant proteins production process.The supply of many polipeptides with potential clinical or industrial use is often limited by their low natural availability. Overexpressed polipeptides may either be located in the cytoplasm and periplasm of E.coli or secreted through the cell membrne into the growth medium.Foreign proteins can be expressed in E.coli cells directly or as fusion proteins with prokaryotic sequences. Frequently, the overexpressed proteins acumulate in the bacterial cytoplasm or periplasm in the form of insoluble inclusion bodies.This review considers isolation, purification, solubiliztion and renaturation of recombinant proteins from E.coli, which is still a serious methodological and technical renaturtion.

Keywords

EN

ESCHERICHIA COLI; GENETIC ENGINEERING; INCLUSION BODY; PROTEIN PURIFICATION; PROTEIN RENATURATION

Discipline

• BIOTECHNOLOGY: BIOTECHNOLOGY

• Publisher: Committee of Biotechnology, Polish Academy of Sciences
• Journal: Biotechnologia
• Year: 1994
• Issue: 4
• Pages: 102-125

Contributors

author

A. Szczepanek

author

A. Plucienniczak

• Document Type: article
• Publication order reference: A.Szczepanek