Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 13, Issue 6, 2006

Page: [555 - 557] Pages: 3

DOI: 10.2174/092986606777145733

Price: $65

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.

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


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy