Cyclitols protect glutamine synthetase and malate dehydrogenase against heat induced deactivation and thermal denaturation
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...
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Published in | Biochemical and biophysical research communications Vol. 345; no. 2; pp. 761 - 765 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
30.06.2006
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Subjects | |
Online Access | Get full text |
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Summary: | 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 (
T
m) of GS from
E. coli by 3.9
°C and MDH from pig heart by 3.4
°C, respectively. Pinitol showed an increase in
T
m of MDH by 3.8
°C, whereas glucose was not effective. Our results show a great potential of stabilizing proteins by the addition of cyclitols. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/j.bbrc.2006.04.144 |