Removal of hydroperoxides by immobilized borohydride: a good method for purification of biochemical materials.
Borohydride was immobilized on a quaternary ammonium type anion exchange resin, Amberlite IRA-400, by an exchange reaction in N,N-dimethylformamide. The reducing ability of borohydride on the polymer beads was examined; 0.1 g resin was applied for about 30 min to 3 ml solutions of hydrogen peroxide, ethyl hydrogen peroxide, and peracetic acid, at a concentration of approximately 40 mM, m-chloroperbenzoic acid (3.13 mM), and 5-phenyl-4-pentenyl-1-hydroperoxide (1 mM), respectively. The solutions were then assayed for remaining hydroperoxide by use of horseradish peroxidase or prostaglandin H synthase. In addition, the effect of treatment on the ability of 5-phenyl-4-pentenyl-1-hydroperoxide to initiate the cyclooxygenase activity of prostaglandin H synthase was investigated. Results indicated that immobilized borohydride is very efficient in removing hydroperoxides. It can be used in either organic or aqueous media. It is convenient for both large and small scales, particularly important for purification of biochemical materials.
Hsuanyu
Y
Y
Department of Chemistry, University of Alberta, Edmonton, Canada.
Dunford
H B
HB
D001894:Borohydrides / Q000737:chemistry*; D002846:Chromatography, Affinity / Q000379:methods*; D006735:Horseradish Peroxidase / Q000378:metabolism; D007475:Ion Exchange Resins / Q000737:chemistry; D010545:Peroxides / Q000032:analysis / Q000737:chemistry*; D011451:Prostaglandin-Endoperoxide Synthases / Q000378:metabolism; D011453:Prostaglandins / Q000378:metabolism
D001894:Borohydrides; D007475:Ion Exchange Resins; D010545:Peroxides; D011453:Prostaglandins; D006735:Horseradish Peroxidase; D011451:Prostaglandin-Endoperoxide Synthases