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Escherichia coli
New findings from Institute of Biochemistry in the area of Escherichia coli published
November 7th, 2009
Scientists discuss in 'Expression and purification of active recombinant equine lysozyme in Escherichia coli' new findings in Escherichia coli. "Equine lysozyme (EL) is a calcium (Ca)-binding lysozyme and is an intermediary link between non-Ca-binding C-type lysozyme and alpha-lactalbumin. The feature of lysozymes to assemble into the fibrils has recently gained considerable attention for the investigation of the functional properties of these proteins," researchers in Vilnius, Lithuania report. "To study the structural and functional properties of EL, a synthetic gene was cloned and EL was overexpressed in Escherichia coli as a fused protein. The His-tagged recombinant EL was accumulated as inclusion bodies. Up to 50 mg/l of the recombinant EL could be achieved after purification by Ni(2+) affinity chromatography, refolding in the presence of arginine, CM-Sepharose column purification following TEV protease cleavage. The purified protein was functionally active, as determined by the lysozyme activity, proving the proper folding of protein. The purified lysozyme was used for the oligomerisation studies. The protein formed amyloid fibrils during incubation in acidic pH and elevated temperature," wrote V. Casaite and colleagues, Institute of Biochemistry. The researchers concluded: "The recombinant EL forms two types of fibrils: ring shaped and linear, similar to the native EL." Casaite and colleagues published their study in Protein Engineering, Design & Selection (Expression and purification of active recombinant equine lysozyme in Escherichia coli. Protein Engineering, Design & Selection, 2009;22(11):649-54). For additional information, contact V. Casaite, Institute of Biochemistry, Dept. of Molecular Microbiology and Biotechnology, Mokslininku 12, Vilnius LT-08662, Lithuania. Publisher contact information for the journal Protein Engineering, Design & Selection is: Oxford University Press, Great Clarendon St., Oxford OX2 6DP, England. Keywords: Lithuania, Vilnius, Biochemistry, Biotechnology, Escherichia coli, Gene Therapy, Genetics, Genomics, Lysozyme, Medical Device, Protein Engineering, Proteomics. This article was prepared by NewsRx editors from staff and other reports. Copyright 2009, NewsRx.com.
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