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Role of Multiple Glutathione Transferases in Bioactivation of Thiopurine Prodrugs Studies of Human Soluble Glutathione Transferases from Alpha, Kappa, Mu, Omega, Pi, Theta, and Zeta Classes
A screening method was developed for identification of catalytically active enzymes in combinatorial cDNA libraries of mutated glutathione transferase (GST) derivatives expressed in E. coli. The method is based on spraying monochlorobimane (MCB) directly over bacterial colonies growing on agar. The substrate MCB become fluorescent under UV light, when the bacterial colony contains acti…
Contributors
- Mannervik Bengt Professor
- Widersten Mikael Docent
- Morgenstern Ralf Professor
- Uppsala universitet Teknisk-naturvetenskapliga vetenskapsområdet Kemiska sektionen Institutionen för naturvetenskaplig biokemi
Creator
- Eklund Birgitta I. 1966- , Uppsala universitet, Institutionen för naturvetenskaplig biokemi
Publisher
- Acta Universitatis Upsaliensis
Date
- 2006
- 2006-09-22
- 2006-08-31
- 2006-08-31
- 2006-09-22
- 2006
Contributors
- Mannervik Bengt Professor
- Widersten Mikael Docent
- Morgenstern Ralf Professor
- Uppsala universitet Teknisk-naturvetenskapliga vetenskapsområdet Kemiska sektionen Institutionen för naturvetenskaplig biokemi
Creator
- Eklund Birgitta I. 1966- , Uppsala universitet, Institutionen för naturvetenskaplig biokemi
Publisher
- Acta Universitatis Upsaliensis
Date
- 2006
- 2006-09-22
- 2006-08-31
- 2006-08-31
- 2006-09-22
- 2006
Providing institution
Aggregator
Rights statement for the media in this item (unless otherwise specified)
- http://rightsstatements.org/vocab/InC/1.0/
- http://rightsstatements.org/vocab/InC/1.0/
Identifier
- oai:DiVA.org:uu-7102
Format
- electronic47
- electronic
- 47
Language
- en
- -1
Is part of
- http://data.theeuropeanlibrary.org/Collection/a1041
Relations
- Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology1651-6214208
Year
- 2006
Providing country
- Sweden
Collection name
First time published on Europeana
- 2014-09-07T11:19:39.095Z
Last time updated from providing institution
- 2014-09-07T11:19:39.095Z