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. 1971 Nov;68(11):2830–2834. doi: 10.1073/pnas.68.11.2830

Partial Purification of Mitochondrial RNA Polymerase from Rat Liver

B D Reid 1, Peter Parsons 1
PMCID: PMC389536  PMID: 5288262

Abstract

Mitochondrial RNA polymerase activity from rat liver has previously been demonstrated in intact organelles. This activity has now been solubilized, partially purified, and shown to be a true polymerase, free of nuclease. The enzyme is derived from mitochondria and is not from contaminating bacteria or nuclear components. The enzyme is distinguished from its nuclear counterparts by its behavior on ammonium sulfate fractionation and lack of inhibition by α-amanitin. Rifamycin inhibits the crude enzyme, but only inconsistently inhibits the more purified preparation.

Keywords: rifampicin, α-amanitin, (NH4)2SO4, DEAE-Sephadex, divalent cations

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Selected References

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