Separation and characterization of the subunits of ribonucleic acid polymerase.

摘要: Abstract This paper presents studies on the subunit structure of Escherichia coli DNA-dependent RNA polymerase. Phosphocellulose column purified enzyme is denatured and its polypeptide chains separated by gel filtration Sephadex G-200 in presence 1% sodium dodecyl sulfate. The amino acid compositions, molecular weights, NH2 terminal acids, molar ratios these are presented. It concluded that phosphocellulose has α2ββ' where weights α, β, β' 39,000 ± 5%, 155,000 10%, 165,000 respectively. In addition, a small protein component, ω, with weight 9,000 10% observed. These subunits not joined together disulfide linkages. From data one can compute 400,000 for monomeric form