Non-Additive Counteraction of KCl-Perturbation of Lactate Dehydrogenase by Trimethylamine N-Oxide

Title: Non-Additive Counteraction of KCl-Perturbation of Lactate Dehydrogenase by Trimethylamine N-Oxide

Volume: 13 Issue: 6

Author(s): Matthew K. Desmond and Joseph F. Siebenaller

Affiliation:

Keywords: Organic osmolytes, counteracting solute hypothesis, compatible solute, porcine muscle-type lactate dehydrogenase

Abstract: 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.

Cite this article as:

Desmond K. Matthew and Siebenaller F. Joseph, Non-Additive Counteraction of KCl-Perturbation of Lactate Dehydrogenase by Trimethylamine N-Oxide, Protein & Peptide Letters 2006; 13 (6) . https://dx.doi.org/10.2174/092986606777145733

DOI https://dx.doi.org/10.2174/092986606777145733	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305