Purification and properties of pyruvate kinase type M1 from bovine brain |
| |
| Authors: | G Terlecki |
| |
| Affiliation: | 1. Department of Cardiovascular Surgery of the First Affiliated Hospital and Institute for Cardiovascular Science, Suzhou Medical College of Soochow University, Soochow University, Suzhou 215007, China;2. State and Local Joint Engineering Laboratory for Novel Functional Polymeric Materials, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, China;1. Faculty of Electrical Engineering and Computing, University of Zagreb, Zagreb, Croatia;2. Wellcome Centre for Integrative Neuroimaging, Oxford Centre for Human Brain Activity, Department of Psychiatry, Warneford Hospital, University of Oxford, United Kingdom;3. Wellcome Centre for Integrative Neuroimaging, Centre for Functional MRI of the Brain (FMRIB), Nuffield Department of Clinical Neurosciences, John Radcliffe Hospital, University of Oxford, United Kingdom;4. Australian Institute for Machine Learning, School of Computer and Mathematical Sciences, The University of Adelaide, Adelaide, SA, Australia;5. South Australian Health and Medical Research Institute (SAHMRI), Adelaide, SA, Australia |
| |
| Abstract: | 1. Pyruvate kinase type M1 was purified from bovine brain about 241-fold with 38% yield. 2. Specific activity of the enzyme was above 217 U/mg of protein (25 degrees C), relative mol. wt of the subunit--57,000 (+/- 2000) and pH optimum--6.8-7.2. 3. The enzyme shoved hyperbolic kinetics with Km value for PEP of 0.04 mM and for ADP of 0.3 mM. 4. Inorganic phosphate and ATP at concentrations below 4 mM showed activating effect, 1-phenylalanine and ATP above 6 mM--an inhibiting effect on the enzyme. 5. Inhibition by 1-phenylalanine was prevented by fructose-1,6-bisphosphate. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
