Abstract
The purification of RNA polymerase from E. coli on single-stranded DNA-agarose columns is described. On these columns the RNA polymerase can be separated into two fractions (1). One fraction contains core enzyme and, though inactive on T4 DNA, a protein with the molecular weight as that of a. The other fraction is shown to be RNA polymerase holo enzyme, based on template specificity and subunit composition. Since σ is not separated from the holo enzyme, this chromatographic method is useful for the preparation of large quantities of holo enzyme.
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