锰取代血红蛋白的制备及其类酶活性的研究  

Preparation and Enzyme-Like Activity Studies of Manganese Reconsitituted-Hemoglobin

作　　者：李得加[1] 蔡小强[1] 王利玲[1] 谢宇翔[1] 李希文[1] 黄俊潮[1] 邹国林[1] 

机构地区：[1]武汉大学生命科学学院,湖北武汉430072

出　　处：《武汉大学学报（理学版）》2004年第2期239-242,共4页Journal of Wuhan University:Natural Science Edition

基　　金：国家自然科学基金资助项目(39770200)

摘　　要：将Mn 原卟啉Ⅸ与脱辅基血红蛋白重组得到Mn取代Fe的重组血红蛋白,用紫外 可见光谱法和SDS PAGE电泳法对Mn取代的血红蛋白进行了鉴定.检测了血红蛋白和Mn取代的血红蛋白的过氧化物酶活性和过氧化氢酶活性.研究发现,Mn取代的血红蛋白的过氧化物酶活性是血红蛋白的70%,过氧化氢酶活性约是血红蛋白的1.9倍.Manganese protoporphyrin IX was recombined with apohemoglobin to prepare artificial hemoglobin containing the manganese porphyrin in place of protoheme or iron protoporphyrin Ⅸ. UV-vis spectra and SDS-PAGE electrophoresis were used to confirm manganese (Ⅲ) protoporphyrin Ⅸ and its apohemoprotein complexes(Mn-Hb)compared with those of the corresponding high spin iron (Ⅲ) compounds. Kinetic studies were carried out with Mn-Hb and hemoglobin to investigate their peroxidase and catalase activity. The experimental results showed that the peroxidase activity of Mn-Hb was 70% of that of hemoglobin, but the catalase activity of Mn-Hb was about 1.9 folds of that of hemoglobin.

关 键 词：锰 血红蛋白 过氧化物酶 过氧化氢酶 紫外-可见光谱法 

分 类 号：Q554.6[生物学—生物化学]