Jump to main content
US EPA
United States Environmental Protection Agency
Search
Search
Main menu
Environmental Topics
Laws & Regulations
About EPA
Health & Environmental Research Online (HERO)
Contact Us
Print
Feedback
Export to File
Search:
This record has one attached file:
Add More Files
Attach File(s):
Display Name for File*:
Save
Citation
Tags
HERO ID
1814194
Reference Type
Journal Article
Title
Hydroperoxidase Activity of Lipoxygenase: A Potential Pathway for Xenobiotic Metabolism in the Presence of Linolenic Acid
Author(s)
Kulkarni, AP; Cook, DC
Year
1988
Is Peer Reviewed?
1
Journal
Research Communications in Chemical Pathology and Pharmacology
ISSN:
0034-5164
Report Number
NIOSH/00183176
Volume
61
Issue
3
Page Numbers
305-314
Abstract
The ability of soybean lipoxygenase to cooxidize xenobiotic compounds was studied in-vitro. Soybean lipoxygenase was incubated with guaiacol (489861) in the presence of linolenic-acid over the pH range 6.0 to 9.0. The rate of oxidation was followed by measuring oxygen consumption and the amount of tetraguaiacol formed. Similar experiments were conducted with boiled lipoxygenase or in the presence of nordihydroguaiaretic-acid (NDGA), an inhibitor of lipoxygenase. Tetramethyl-p-phenylenediamine (100221) (TMPD), tetramethylbenzidine (366290) (TMB), benzidine (92875), dimethoxybenzidine (119904) (DMB), p-phenylene-diamine (106503) (PPD), or 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic-acid) (30931670) (ABTS) were incubated with soybean lipoxygenase and linolenic-acid and the extent of cooxidation and hydroperoxidase activity were determined as before. Maximum formation of tetraguaiacol occurred at pH 9.0. The amount of tetraguaiacol formed depended on the amount of lipoxygenase and the concentrations of guaiacol and linolenic-acid used. Consumption of oxygen did not depend on the concentration of guaiacol. Boiled lipoxygenase had no hydroperoxidase activity. NDGA inhibited formation of tetraguaiacol in a dose dependent manner. TMPD, TMB, benzidine, DMB, PPD, and ABTS were all cooxidized by lipoxygenase and linolenic-acid. Lipoxygenase had the greatest hydroperoxidase activity toward DMB and the least toward benzidine. The authors conclude that the hydroperoxidase activity of soybean lipoxygenase has a wide substrate specificity and may be a potential pathway of xenobiotic oxidation.
Keywords
DCN-171978
;
In vitro studies
;
Agricultural products
;
Enzyme activity
;
Oxidative processes
;
Oxygen uptake
;
Fatty acids
;
Biotransformation
;
Organic compounds
Home
Learn about HERO
Using HERO
Search HERO
Projects in HERO
Risk Assessment
Transparency & Integrity