Abstract
A strategy has been developed and optimized that allows the isolation of proteins of the large subunit fromEscherichia coliribosomes 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.
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