Báo cáo khoa học: Perturbation of folding and reassociation of lactate dehydrogenase by proline and trimethylamine oxide
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Investigations of protein–solute interactions typically showthat osmolytes favor native conformations. In this study,the effects of representative compatible and counteractingosmolytes on the reactivationof lactate dehydrogenase fromtwo different conformational states were explored. Contraryto expectations, proline and trimethylamine oxide inhibitedboth the initial time course and the extent of reactivation oflactate dehydrogenase from bovine heart following dena-turation in guanidine hydrochloride, as well as followinginactivation at pH 2.3. Reactivation of acid-dissociatedporcine heart lactate dehydrogenase was inhibited by bothproline and trimethylamine oxide (2M). In all instances,trimethylamine oxide was the more effective inhibitor ofreactivation. ...
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Báo cáo khoa học: Perturbation of folding and reassociation of lactate dehydrogenase by proline and trimethylamine oxide
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Báo cáo khoa học: Perturbation of folding and reassociation of lactate dehydrogenase by proline and trimethylamine oxide
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