辣根过氧化物酶催化的乙醇醛对蛋白质加合物的化学发光需氧氧化反应。

Chemiluminescent aerobic oxidation of protein adducts with glycolaldehyde catalyzed by horseradish peroxidase.

作者信息

de Medeiros M H, Bechara E J

出版信息

Arch Biochem Biophys. 1986 Jul;248(1):435-9. doi: 10.1016/0003-9861(86)90441-8.

Abstract

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.

摘要

辣根过氧化物酶（EC 1.11.1.7）在生理pH值下可催化溶菌酶、牛血清白蛋白和鱼精蛋白与乙醇醛加合物的有氧氧化反应。该反应伴有发光现象，这归因于三线态物种的产生。添加溶解在Brij 35中的叶绿素α可增强化学发光强度。文中提出电子激发态物种在与席夫型加合物形成相关的有害和病理过程中所起的作用，重点讨论了酒精性肝损伤的情况。