Affinity isolation of RNA polymerase II on amanitin-Sepharose

Lutter , Leonard C.; Faulstich, Heinz

doi:10.1016/0006-291X(84)91615-2

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Affinity isolation of RNA polymerase II on amanitin-Sepharose

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Faulstich, Heinz
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0006291X84916152/pdf?md5=bfc6d186985e0e9b23c5884072008a15&pid=1-s2.0-0006291X84916152-main.pdf
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Citation

Lutter, L. C., & Faulstich, H. (1984). Affinity isolation of RNA polymerase II on amanitin-Sepharose. Biochemical and Biophysical Research Communications, 119(1), 42-48. doi:10.1016/0006-291X(84)91615-2.

Cite as: https://hdl.handle.net/21.11116/0000-0006-8D60-F

Abstract

We report here the first case of an affinity isolation of eukaryotic RNA polymerase II. The procedure employs an affinity matrix composed of α-amanitin coupled to Sepharose 4B via a ten atom spacer. RNA polymerase II from either calf thymus or wheat germ binds to the amanitin-Sepharose, as indicated by subsequent elution with sodium dodecylsulfate-containing buffer and analysis by polyacrylamide gel electrophoresis. The specificity of binding is demonstrated by the fact that when the enzyme is preincubated with 1 μg/ml of free α-amanitin, subsequent binding to the amanitin-Sepharose is abolished. Elution methods that should permit the recovery of active enzyme from the column are discussed.