Large-scale isolation of proteins of the large subunit from Escherichia coli ribosomes.
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.
Diedrich
G
G
Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Berlin, Germany.
Burkhardt
N
N
Nierhaus
K H
KH
D000837:Anion Exchange Resins; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002411:Cation Exchange Resins; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry*; D007475:Ion Exchange Resins; D012117:Resins, Synthetic; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D012270:Ribosomes / Q000737:chemistry*
D000837:Anion Exchange Resins; D001426:Bacterial Proteins; D002411:Cation Exchange Resins; D007475:Ion Exchange Resins; C106553:Mono-S; D012117:Resins, Synthetic; D012269:Ribosomal Proteins; C042855:Mono Q