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dc.contributor.authorTuntland ML
dc.contributor.authorFung LW-M
dc.date.accessioned2016-12-15T18:57:25Z
dc.date.available2017-12-16T10:30:05Z
dc.date.issued2016-07
dc.identifier.bibliographicCitationTuntland, M. L. and Fung, L. W. M. Substrate Independent ATPase Activity May Complicate High Throughput Screening.. Analytical Biochemistry. 2016. 510: 18-20. doi: 10.1016/j.ab.2016.07.016.en_US
dc.identifier.issn0003-2697
dc.identifier.urihttp://hdl.handle.net/10027/21400
dc.descriptionThis is the author’s version of a work that was accepted for publication in Analytical Biochemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Analytical Biochemistry, 2016. 510: 18-20. DOI: 10.1016/j.ab.2016.07.016.en_US
dc.description.abstractInorganic phosphate release, [Pi], is often measured in an enzymatic reaction in a high throughput setting. Based on the published mechanism, we designed a protocol for our screening for inhibitors of SAICAR synthetase (PurC), and we found a gradual increase in [Pi] in positive control samples over the course of the day. Further investigation indicated that hydrolysis of ATP catalyzed by PurC, rather than substrate-related phosphate release, was responsible for a partial contribution to the signals in the control samples. Thus substrate-independent ATPase activity may complicate high throughput screeningen_US
dc.description.sponsorshipThe work was supported, in part, by a grant from the National Institutes of Health (U19 AI-56575).en_US
dc.publisherElsevier Massonen_US
dc.subjectMalachite greenen_US
dc.subjectHigh throughput screeningen_US
dc.subjectSubstrate-independent ATPase activityen_US
dc.titleSubstrate Independent ATPase Activity May Complicate High Throughput Screening.en_US
dc.typeArticleen_US


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