Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 2006 Jun 30;345(2):761-5. Epub 2006 May 3.

Cyclitols protect glutamine synthetase and malate dehydrogenase against heat induced deactivation and thermal denaturation.

Author information

1
Department of Biomolecular Structural Chemistry, University of Vienna, A-1030 Vienna, Austria. martina.jaindl@univie.ac.at

Abstract

The accumulation of cyclitols in plants is a widespread response that provides protection against various environmental stresses. The capacity of myo-Inositol, pinitol, quercitol, and other compatible solutes (i.e., sorbitol, proline, and glycinebetaine) to protect proteins against thermally induced denaturation and deactivation was examined. Enzymatic activity measurements of L-glutamine synthetase from Escherichia coli and Hordeum vulgare showed that the presence of cyclitols during heat treatment resulted in a significantly higher percentage of residual activity. CD spectroscopy experiments were used to study thermal stabilities of protein secondary structures upon the addition of myo-Inositol, pinitol, and glucose. 0.4 M myo-Inositol was observed to raise the melting temperature (Tm) of GS from E. coli by 3.9 degrees C and MDH from pig heart by 3.4 degrees C, respectively. Pinitol showed an increase in Tm of MDH by 3.8 degrees C, whereas glucose was not effective. Our results show a great potential of stabilizing proteins by the addition of cyclitols.

PMID:
16701563
DOI:
10.1016/j.bbrc.2006.04.144
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center