Non-additive counteraction of KCl-perturbation of lactate dehydrogenase by trimethylamine N-oxide
Added KCl increases the apparent Michaelis constant (Km) of pyruvate for porcine muscle-type lactate dehydrogenase (100 mM KCl, 83%; 200 mM KCl, 188%). The effects of 100 mM KCl were fully reversed by 375 mM trimethylamine N-oxide (TMAO). TMAO (375-750 mM) partially reversed the effects of 200 mM KCl. TMAO as the sole solute, at concentrations up to 750 mM, had no effect on Km. This is atypical because compensatory osmolytes such as TMAO characteristically counteract protein perturbation in an additive manner. © 2006 Bentham Science Publishers Ltd.
Publication Source (Journal or Book title)
Protein and Peptide Letters
Desmond, M., & Siebenaller, J. (2006). Non-additive counteraction of KCl-perturbation of lactate dehydrogenase by trimethylamine N-oxide. Protein and Peptide Letters, 13 (6), 555-557. https://doi.org/10.2174/092986606777145733