Hen heart AMP-deaminase--the combined effect of ATP, ADP and orthophosphate on the enzyme activity |
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| Authors: | K Kaletha |
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| Affiliation: | 1. Department of Labor Law, Yaroslav Mudryi National Law University, 61024, 77 Pushkinska Str., Kharkiv, Ukraine;2. Department of State Building, Yaroslav Mudryi National Law University, 61024, 77 Pushkinskaya Str., Kharkiv, Ukraine;1. Mechanical Engineering Department, Faculty of Engineering, Kafrelsheikh University, Kafrelsheikh, 33516, Egypt;2. New Cairo Technological University, Cairo, 11511, Egypt;3. Higher Institute of Engineering and Technology, Kafrelsheikh, Egypt;1. Department of Economics, Sociology and Agrarian Policy, University of Cordoba Spain, Edificio Gregor Mendel, 14071, Córdoba, Spain;2. Departamento de Métodos Cuantitativos, University Loyola Spain, C/ Escritor Castilla Aguayo, 4 14004, Córdoba, Spain;3. Department of Spanish and International Economy, Econometrics and History and Economic Institutions, University of Castilla-La Mancha, Plaza de la Universidad, nº 1, 02071, Albacete, Spain;1. Division of Allergy and Immunology, Center for Food Allergy, Department of Pediatrics, University of Rochester School of Medicine and Dentistry, Golisano Children’s Hospital, Rochester, NY;2. TurtleTree LLC, Woodland, Calif;3. Department of Food Science, University of Massachusetts Amherst, Amherst, Mass;5. Organismic and Evolutionary Biology Graduate Program, University of Massachusetts Amherst, Amherst, Mass;4. Department of Microbiology and Physiological Systems, University of Massachusetts Chan Medical School, Worcester, Mass;6. Department of Biomedical Sciences, University of Albany, Rensselaer, NY;7. Division of Infectious Diseases, New York State Department of Health, Albany, NY;8. Division of Allergy, Immunology, and Rheumatology, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY;9. Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, NY;1. Department of Chemistry, University of Michigan, Ann Arbor, Michigan, USA;2. Department of Chemical Engineering, Virginia Polytechnic Institute and State University, Blacksburg, Virginia, USA;3. Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA;1. Department of Pharmacology, Toxicology and Clinical Pharmacology, Faculty of Medicine, University of Banja Luka, Banja Luka, Republic of Srpska, Bosnia and Herzegovina;2. Experta Consulting, Belgrade, Serbia;3. Department of Anesthesiology and Intensive Care, Institute for Cardiovascular Diseases, Dedinje, Belgrade, Serbia |
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| Abstract: | Interpretation of the kinetic data in terms of concerted transition theory indicated that in the presence of 100 mM potassium chloride hen heart AMP-deaminase may be active as a dimer. The presence of ATP, but not of the ADP in the incubation medium shifts completely the allosteric equilibrium towards the active, accessible to the substrate form of the enzyme. In the joint presence of main enzyme effectors (ATP, ADP and orthophosphate) added to the incubation medium at physiological concentrations, the plot of the reaction rate versus substrate concentration manifested hyperbolic dependence and the value of half-saturation constant (K0.5) did not differ from the value of this parameter obtained for ATP(alone)-activated enzyme. |
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