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Mendeley readers
Chapter title |
Purification of Recombinant Human PARG and Activity Assays
|
---|---|
Chapter number | 25 |
Book title |
Poly(ADP-Ribose) Polymerase
|
Published in |
Methods in molecular biology, July 2017
|
DOI | 10.1007/978-1-4939-6993-7_25 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6992-0, 978-1-4939-6993-7
|
Authors |
Jean-Christophe Amé, Éléa Héberlé, Barbara Camuzeaux, Françoise Dantzer, Valérie Schreiber |
Abstract |
The purification of Poly(ADP-ribose) glycohydrolase (PARG) from overexpressing bacteria Escherichia coli is described here to a fast and reproducible one chromatographic step protocol. After cell lysis, GST-PARG-fusion proteins from the crude extract are affinity purified by a Glutathione 4B Sepharose chromatographic step. The PARG proteins are then freed from their GST-fusion by overnight enzymatic cleavage using the preScission protease. As described in the protocol, more than 500 μg of highly active human PARG can be obtained from 1.5 L of E. coli culture. |
Mendeley readers
The data shown below were compiled from readership statistics for 8 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 8 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 2 | 25% |
Professor | 1 | 13% |
Student > Ph. D. Student | 1 | 13% |
Student > Doctoral Student | 1 | 13% |
Unknown | 3 | 38% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 4 | 50% |
Unknown | 4 | 50% |