Murdoch University Research Repository

Welcome to the Murdoch University Research Repository

The Murdoch University Research Repository is an open access digital collection of research
created by Murdoch University staff, researchers and postgraduate students.

Learn more

Using N,N,N’,N’-tetramethyl-p-phenylenediamine (TMPD) to Assay Cyclooxygenase Activity In Vitro

Petrovic, N. and Murray, M. (2009) Using N,N,N’,N’-tetramethyl-p-phenylenediamine (TMPD) to Assay Cyclooxygenase Activity In Vitro. Methods in molecular biology, 594 . pp. 129-140.

Link to Published Version:
*Subscription may be required


Prostaglandin endoperoxide synthase (PGH synthase), also known as cyclooxygenase (COX), was identified over 30 years ago and is the key enzyme in the pathway by which arachidonic acid is converted to the range of biologically active lipid mediators known as the prostanoids that participate in numerous physiological processes. The need for the development of new and improved COX inhibitors as potential therapeutics also drives the need for rapid, reliable, and inexpensive assays of COX activity. Colorimetric assays are often the preferred methods of enzyme analysis since they may be readily adapted to simple microplate formats that require relatively inexpensive and widely available instrumentation. The use of N,N,N cent,N cent-tetramethyl-p-phenylenediamine (TMPD) in high throughput microplate assays of COX activity could become the approach of choice in the screening of potential therapeutics that inhibit COX activity in vivo. Considering that TMPD is also a potential substrate for most, if not all, heme peroxidases, it is anticipated that this agent could find increasing application in the future.

Item Type: Journal Article
Murdoch Affiliation(s): School of Pharmacy
Publisher: Humana Press, Inc.
Item Control Page Item Control Page