锰取代血红蛋白的制备及其类酶活性的研究

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 李得加 LI De-jia 1 2 first-author 蔡小强 CAI Xiao-qiang 1 2 王利玲 WANG Li-ling 1 2 谢宇翔 XIE Yu-xiang 1 2 李希文 LI Xi-wen 1 2 黄俊潮 HUANG Jun-chao 1 2 邹国林 ZOU Guo-lin 1 2 武汉大学生命科学学院 武汉大学生命科学学院 College of Life Sciences, Wuhan University College of Life Sciences, Wuhan University 武汉大学生命科学学院,湖北,武汉,430072 武汉大学生命科学学院,湖北,武汉,430072 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. 血红蛋白 锰 过氧化物酶 过氧化氢酶 hemoglobin manganese peroxidase catalase Q554.6 国家自然科学基金资助项目（39770200） 2004-02-01 2021-04-01 2