Please use this identifier to cite or link to this item: http://dlib.scu.ac.ir/handle/2027.42/24897
Title: Affinity isolation of RNA polymerase II on amanitin-Sepharose
Authors: Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA;Department of Chemistry of Natural Products Max Planck Institute for Medical Research, Heidelberg, West Germany
Publisher: Elsevier
Description: We report here the first case of an affinity isolation of eukaryotic RNA polymerase II. The procedure employs an affinity matrix composed of [alpha]-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 [mu]g/ml of free [alpha]-amanitin, subsequent binding to the amanitin-Sepharose is abolished. Elution methods that should permit the recovery of active enzyme from the column are discussed.
URI: https://deepblue.lib.umich.edu/handle/2027.42/24897
More Information: Lutter, Leonard C., Faulstich, Heinz (1984/02/29)."Affinity isolation of RNA polymerase II on amanitin-Sepharose." Biochemical and Biophysical Research Communications 119(1): 42-48. <http://hdl.handle.net/2027.42/24897>
http://www.sciencedirect.com/science/article/B6WBK-4DNJ692-2T7/2/a740acfdf5d7be5f18a5209bb620c7ae
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6704131&dopt=citation
http://hdl.handle.net/2027.42/24897
6704131
http://dx.doi.org/10.1016/0006-291X(84)91615-2
Biochemical and Biophysical Research Communications
Appears in Collections:Research Collections

Files in This Item:
Click on the URI links for accessing contents.
Title: Affinity isolation of RNA polymerase II on amanitin-Sepharose
Authors: Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA;Department of Chemistry of Natural Products Max Planck Institute for Medical Research, Heidelberg, West Germany
Publisher: Elsevier
Description: We report here the first case of an affinity isolation of eukaryotic RNA polymerase II. The procedure employs an affinity matrix composed of [alpha]-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 [mu]g/ml of free [alpha]-amanitin, subsequent binding to the amanitin-Sepharose is abolished. Elution methods that should permit the recovery of active enzyme from the column are discussed.
URI: https://deepblue.lib.umich.edu/handle/2027.42/24897
More Information: Lutter, Leonard C., Faulstich, Heinz (1984/02/29)."Affinity isolation of RNA polymerase II on amanitin-Sepharose." Biochemical and Biophysical Research Communications 119(1): 42-48. <http://hdl.handle.net/2027.42/24897>
http://www.sciencedirect.com/science/article/B6WBK-4DNJ692-2T7/2/a740acfdf5d7be5f18a5209bb620c7ae
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6704131&dopt=citation
http://hdl.handle.net/2027.42/24897
6704131
http://dx.doi.org/10.1016/0006-291X(84)91615-2
Biochemical and Biophysical Research Communications
Appears in Collections:Research Collections

Files in This Item:
Click on the URI links for accessing contents.
Title: Affinity isolation of RNA polymerase II on amanitin-Sepharose
Authors: Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA;Department of Chemistry of Natural Products Max Planck Institute for Medical Research, Heidelberg, West Germany
Publisher: Elsevier
Description: We report here the first case of an affinity isolation of eukaryotic RNA polymerase II. The procedure employs an affinity matrix composed of [alpha]-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 [mu]g/ml of free [alpha]-amanitin, subsequent binding to the amanitin-Sepharose is abolished. Elution methods that should permit the recovery of active enzyme from the column are discussed.
URI: https://deepblue.lib.umich.edu/handle/2027.42/24897
More Information: Lutter, Leonard C., Faulstich, Heinz (1984/02/29)."Affinity isolation of RNA polymerase II on amanitin-Sepharose." Biochemical and Biophysical Research Communications 119(1): 42-48. <http://hdl.handle.net/2027.42/24897>
http://www.sciencedirect.com/science/article/B6WBK-4DNJ692-2T7/2/a740acfdf5d7be5f18a5209bb620c7ae
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6704131&dopt=citation
http://hdl.handle.net/2027.42/24897
6704131
http://dx.doi.org/10.1016/0006-291X(84)91615-2
Biochemical and Biophysical Research Communications
Appears in Collections:Research Collections

Files in This Item:
Click on the URI links for accessing contents.