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- W2016402094 abstract "Abstract DNA-dependent RNA polymerases type A and B from rat liver nuclei were found to be inactivated by a macromolecular inhibitor. This inhibitor was located mainly in the smooth rat liver endoplasmic reticulum. The extraction of this substance from smooth microsomal membranes was carried out with 0.1% sodium deoxycholate and 0.2 M (NH4)2SO4. Purification of the inhibitor was achieved by chromatography on DEAE-cellulose followed by ECTEOLA-cellulose and DEAE-Sephadex chromatography. Evidence for the macromolecular nature of the inhibitor was obtained by gel filtration and heat stability experiments. The inhibitory effect was not connected with RNAase, DNAase, or with enzymic hydrolysis of the various nucleoside triphosphates acting as nucleoside triphosphatase or nucleoside triphosphate pyrophosphatase. Complete inhibition with both A and B polymerases was observed. However, polymerase A activity was more sensitive to the inhibitor. The inhibitory effect is related to the concentration of managanese and all four nucleoside triphosphates present in the assay. These data support the possibility that the inhibitor binds the Mn2+-nucleoside triphosphate complex thus preventing the substrate from reaching the enzyme site(s)." @default.
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- W2016402094 title "A macromolecular inhibitor of rat liver DNA-dependent RNA polymerases" @default.
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- W2016402094 doi "https://doi.org/10.1016/0005-2787(77)90275-1" @default.
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