Chemiluminescent aerobic oxidation of protein adducts with glycolaldehyde catalyzed by horseradish peroxidase.
Horseradish peroxidase (EC 1.11.1.7) is shown to catalyze the aerobic oxidation of lysozyme, bovine serum albumin, and protamine adducts with glycolaldehyde at physiological pH. This reaction is accompanied by light emission, which is attributed to the generation of triplet species. The intensity of chemiluminescence is enhanced by addition of chlorophyll alpha solubilized in Brij 35. A role of electronically excited species in deleterious and pathological processes associated with formation of Schiff-type adducts is suggested, with emphasis on the case of alcohol-induced liver injury.
D000079:Acetaldehyde / Q000031:analogs & derivatives* / Q000378:metabolism; D002734:Chlorophyll / Q000494:pharmacology; D000077194:Chlorophyll A; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D008163:Luminescent Measurements; D009113:Muramidase / Q000378:metabolism; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D010544:Peroxidases / Q000378:metabolism*; D000077423:Polidocanol; D011092:Polyethylene Glycols; D011479:Protamines / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013053:Spectrophotometry
D011479:Protamines; D011506:Proteins; D000077423:Polidocanol; D002734:Chlorophyll; D012710:Serum Albumin, Bovine; D011092:Polyethylene Glycols; D006735:Horseradish Peroxidase; D010544:Peroxidases; D009113:Muramidase; D000079:Acetaldehyde; D010100:Oxygen; C010972:glycolaldehyde; D000077194:Chlorophyll A