TAILIEUCHUNG - Báo cáo khoa học: Perturbation of folding and reassociation of lactate dehydrogenase by proline and trimethylamine oxide

Investigations of protein–solute interactions typically show that osmolytes favor native conformations. In this study, the effects of representative compatible and counteracting osmolytes on the reactivationof lactate dehydrogenase from two different conformational states were explored. Contrary to expectations, proline and trimethylamine oxide inhibited both the initial time course and the extent of reactivation of lactate dehydrogenase from bovine heart following dena-turation in guanidine hydrochloride, as well as following inactivation at pH . Reactivation of acid-dissociated porcine heart lactate dehydrogenase was inhibited by both proline and trimethylamine oxide (2M). In all instances, trimethylamine oxide was the more effective inhibitor of reactivation. . | Eur. J. Biochem. 270 4823-4834 2003 FEBS 2003 doi Perturbation of folding and reassociation of lactate dehydrogenase by proline and trimethylamine oxide Oscar P. Chilson and Anne E. Chilson Department of Biology Washington University St Louis MO USA Investigations of protein-solute interactions typically show that osmolytes favor native conformations. In this study the effects of representative compatible and counteracting osmolytes on the reactivation of lactate dehydrogenase from two different conformational states were explored. Contrary to expectations proline and trimethylamine oxide inhibited both the initial time course and the extent of reactivation of lactate dehydrogenase from bovine heart following denaturation in guanidine hydrochloride as well as following inactivation at pH . Reactivation of acid-dissociated porcine heart lactate dehydrogenase was inhibited by both proline and trimethylamine oxide 2 m . In all instances trimethylamine oxide was the more effective inhibitor of reactivation. Analysis of the catalytic properties of the reactivating enzyme provided evidence that the molecular species that was enzymatically active during the initial stages of reactivation of acid-inactivated porcine heart lactate dehydrogenase reflects a non-native conformation. Proline and trimethylamine oxide stabilize polypeptides through exclusion from the polypeptide backbone the inhibition of renaturation reassociation described here is probably due to attenuation of this stabilizing influence through favorable interactions of the osmolytes with sidechains of residues that lie at the interfaces of the monomers and dimers that associate to form the active tetramer. In addition these osmo-lytes may stabilize non-native intermediates in the folding pathway. The high viscosity of solutions containing more than 3 M proline was a major factor in the inhibition of reassociation of acid-dissociated porcine heart lactate dehydrogenase as .

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