Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10534090 | Analytical Biochemistry | 2005 | 7 Pages |
Abstract
A high-throughput screening method based on the competitive binding of a lumazine synthase inhibitor and riboflavin to the active site of Schizosaccharomyces pombe lumazine synthase was developed. This assay is sensitive, simple, and robust. During assay development, all of the known active inhibitors tested were positively identified. Preliminary high-throughput screening in 384-well format resulted in a Z factor of 0.7. The approach utilizes a thermodynamic assay to bypass the problems associated with the instabilities of both lumazine synthase substrates that complicate the use of a kinetic assay in a high-throughput format, and it removes the time element from the assay, thus simplifying the procedure.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Jinhua Chen, Boris Illarionov, Adelbert Bacher, Markus Fischer, Ilka Haase, Gunda Georg, Qi-zhuang Ye, Zeqiang Ma, Mark Cushman,