Colorimetric determination of pure Mg2+-dependent phosphatidate phosphatase activity

Tara Havriluk, Fred Lozy, Symeon Siniossoglou, George M. Carman

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

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).

Original languageEnglish (US)
Pages (from-to)392-394
Number of pages3
JournalAnalytical Biochemistry
Volume373
Issue number2
DOIs
StatePublished - Feb 15 2008

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Colorimetric determination of pure Mg2+-dependent phosphatidate phosphatase activity'. Together they form a unique fingerprint.

Cite this