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.
出处
《武汉大学学报(理学版)》
CAS
CSCD
北大核心
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)