Rapid purification of adenylate kinase from human erythrocytes and skeletal muscle |
| |
| Institution: | 1. Department of Pharmacology and Toxicology, University of Graz, Graz 8010, Austria;2. Cardiovascular Division and Lillehei Heart Institute, University of Minnesota, Minneapolis, MN 55455, USA;3. Department of Exercise Rehabilitation, Shanghai University of Sport, Shanghai 200438, China;4. Division of Cardiology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD, USA;1. The Key Laboratory of Cardiovascular Remodeling and Function Research, Chinese Ministry of Education，Chinese Ministry of Health and Chinese Academy of Medical Sciences, The State and Shandong Province Joint Key Laboratory of Translational Cardiovascular Medicine, Qilu Hospital of Shandong University, Jinan, Shandong, China;2. School of Pharmacy, Hubei University of Science and Technology, Xianning, Hubei, China;3. Department of General Surgery, Qilu Hospital of Shandong University, Jinan, China;4. School of Life Science, Key Laboratory of the Ministry of Education for Experimental Teratology, Shandong University, Jinan, China;1. Division of Gynecologic Oncology, Duke Cancer Institute, United States of America;2. Division of Gynecologic Oncology, Virginia Oncology Associates, United States of America;3. Department of Biostatistics and Bioinformatics, Duke Cancer Institute, United States of America;4. Division of Gynecologic Oncology, University of Virginia, United States of America;5. Department of Medicine, Duke Cancer Institute, Durham, NC 27710, United States of America |
| |
| Abstract: | Adenylate kinase from human erythrocytes and skeletal muscle can be purified to homogeneity by a new procedure based on DEAE-Sepharose and Blue Sepharose affinity chromatography and Sephadex G-75 fractionation. For the enzyme purified from erythrocytes the specific activity is 3000 U/mg of protein, and the overall yield is 70%. For the enzyme purified from skeletal muscle the specific activity is 2075 U/mg of protein, and the overall yield is 44%. The sequence of steps takes advantage of the high isoelectric point, the high affinity for Blue Sepharose, and the low molecular weight of the isoenzyme from these two human tissues. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
