ESTERASE COUPLED WITH THE H2O2 HORSERADISH PEROXIDASE SYSTEM TRIGGERSCHEMILUMINESCENCE FROM 2-METHYL-1-PROPENYLBENZOATE - A POTENTIAL ANALYTICAL TOOL FOR ESTERASE ANALYSIS/
B. Yavo et al., ESTERASE COUPLED WITH THE H2O2 HORSERADISH PEROXIDASE SYSTEM TRIGGERSCHEMILUMINESCENCE FROM 2-METHYL-1-PROPENYLBENZOATE - A POTENTIAL ANALYTICAL TOOL FOR ESTERASE ANALYSIS/, Analytical biochemistry, 234(2), 1996, pp. 215-220
The hydrolysis of 2-methyl-1-propenylbenzoate catalyzed by esterase pr
oduces 2-methyl-1-propenol, which can be subsequently oxidized by the
H2O2/horseradish peroxidase (HRP) system to yield electronically excit
ed triplet acetone. The level of luminescence elicited by this species
is proportional to total esterase used, making it possible to determi
ne as little as 2 pmol of esterase. Yet, its intensity can be enhanced
several orders of magnitude by fluorescent accepters like sodium 9,10
-dibromoanthracene-2-sulfonate. The system works as a chemiluminescent
reaction triggered by esterase and can be used to elaborate analytica
l assays to determine its activity. This chemiluminescence is also pro
moted by HRP conjugates instead of free HRP and, hence, this simple re
action system can also be used to develop sensitive chemiluminescent i
mmunoassays based upon peroxidase activity. (C) 1996 Academic Press, I
nc.