Substrate independent ATPase activity may complicate high throughput screening |
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Authors: | Micheal L Tuntland LW-M Fung |
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Institution: | Department of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA |
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Abstract: | Inorganic 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 screening. |
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Keywords: | Malachite green High throughput screening Substrate-independent ATPase activity |
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