Large-scale isolation of proteins of the large subunit from Escherichia coli ribosomes

Protein Expression and Purification
G DiedrichK H Nierhaus

Abstract

A strategy has been developed and optimized that allows the isolation of proteins of the large subunit from Escherichia coli ribosomes and combines the following advantages: speed, applicability for the isolation of milligram amounts of a single protein, and preservation of the biological activity of the proteins. The method consists of the following steps: ion-exchange chromatography on MonoS and MonoQ, gel filtration on Sephadex 75, and salt washes. Eleven proteins can be purified by a single chromatographic step, and a combination of two steps enables the isolation of the other proteins.

References

Jun 1, 1991·Biochimie·K H Nierhaus
Jan 1, 1988·Methods in Enzymology·B S CoopermanM A Buck
Dec 6, 1994·Proceedings of the National Academy of Sciences of the United States of America·D I SvergunM H Koch

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Citations

Jan 6, 2007·Journal of Proteome Research·William E RunningJames P Reilly
Apr 26, 2000·Proceedings of the National Academy of Sciences of the United States of America·U StelzlK H Nierhaus
Feb 28, 2002·Methods : a Companion to Methods in Enzymology·U Stelzl, K H Nierhaus
Dec 9, 2010·Archives of Natural History·C T Ambrose
May 10, 2003·The Journal of Biological Chemistry·Ulrich StelzlDinshaw J Patel
Dec 15, 2000·Journal of Molecular Biology·R WillumeitK H Nierhaus
Jul 27, 2001·Biochimica Et Biophysica Acta·R WillumeitK H Nierhaus
Jan 31, 2009·Journal of Proteome Research·William E Running, James P Reilly

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