Thermal stability of horse liver alcohol dehydrogenase and its complexes |
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| Authors: | H Theorell K Tatemoto |
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| Affiliation: | 1. Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET-UNR), Rosario, Argentina;2. Area Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina;1. Structural Heart and Valve Center, Center for Interventional Vascular Therapy, Division of Cardiology, Columbia University Medical Center, New York, NY, United States;2. Brown University, Providence, RI, United States;3. Icahn School of Medicine at Mount Sinai, New York, NY, United States;4. Massachusetts General Hospital, Boston, MA, United States;5. Brigham and Women''s Hospital, Boston, MA, United States |
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| Abstract: | Horse liver alcohol dehydrogenase (LADH) was protected against thermal denaturation by addition of NADH or NAD+ and further protected by NADH + isobutyramide or NAD+ + pyrazole. The effect was increased with increasing concentration of the ligand(s), indicating that the protection of LADH is dependent on equilibrium of the reaction between the enzyme and the ligand(s). The dissociation constants and the denaturation-rate constants of LADH complexes were determined from the thermal denaturation curves. |
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