Journal
ANALYTICAL BIOCHEMISTRY
Volume 373, Issue 2, Pages 392-394Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2007.08.037
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Funding
- Medical Research Council [G0701446] Funding Source: Medline
- NIGMS NIH HHS [R01 GM028140, R01 GM028140-25, GM-28140, R37 GM028140] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- Medical Research Council [G0701446] Funding Source: researchfish
- MRC [G0701446] Funding Source: UKRI
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The malachite green-molybdate reagent was used for a colorimetric assay of pure Mg2(+)-dependent phosphatidate phosphatase activity. This enzyme plays a major role in fat metabolism. Enzyme activity was linear with time and protein concentration, and with the concentration of water-soluble dioctanoyl phosphatidate. The colorimetric assay was used to examine enzyme inhibition by phenylglyoxal, propranolol, and dimethyl sulfoxide. Pure enzyme and a water-soluble phosphatidate substrate were required for the assay, which should be applicable to a well-defined large-scale screen of Mg2(+)-dependent phosphatidate phosphatise inhibitors (or activators). (C) 2007 Elsevier Inc. All rights reserved.
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