Creatinine amidohydrolase: Some properties of the partially purified and purified enzyme |
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| Affiliation: | 1. Department of Mathematics, Sethu Institute of Technology, Pulloor, Kariapatti-626115, Tamil Nadu, India;2. Department of Analytical Chemistry, School of Pharmacy and Life Sciences, Robert Gordon University, Aberdeen, UK;1. School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, PR China;2. Department of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310027, PR China;3. Zunyi Medical College (Zhuhai Campus), Zhuhai, 519041, PR China;1. Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK;1. Department of Laboratory Medicine, Yale School of Medicine, New Haven, CT, United States;2. Department of Pathology, Yale School of Medicine, New Haven, CT, United States |
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| Abstract: | - 1.1. Creatinine amidohydrolase from Pseudomonas sp. has a pH optimum of 8.0 and is activated by divalent metals manganese, magnesium, zinc and cobalt.
- 2.2. It is acid labile but shows good stability at 55°C in alkaline solutions.
- 3.3. It has a mol. wt in the region of 248,000 and Michaelis constants of 31.7mM and 80 mM for creatinine and creatine respectively.
- 4.4. Results indicate that the enzyme molecule contains 8 subunits of similar mol. wt.
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