Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase

Hall D.R., Jacobsen M.P. and Winzor D.J. (1995) Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase. Biophysical Chemistry, 57 1: 47-54. doi:10.1016/0301-4622(95)00044-X


Author Hall D.R.
Jacobsen M.P.
Winzor D.J.
Title Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase
Journal name Biophysical Chemistry   Check publisher's open access policy
ISSN 0301-4622
Publication date 1995-01-01
Sub-type Article (original research)
DOI 10.1016/0301-4622(95)00044-X
Open Access Status Not yet assessed
Volume 57
Issue 1
Start page 47
End page 54
Total pages 8
Subject 1303 Specialist Studies in Education
1304 Biophysics
1605 Policy and Administration
1606 Political Science
Abstract Measurements of the kinetics of activity loss by rabbit muscle lactate dehydrogenase in acetate-chloride buffer, pH 5.0, I 0.20, have shown that the enzyme exhibits greater stability against irreversible inactivation when the buffer is supplemented with sucrose (0.1 M-0.5 M). On the basis of sedimentation equilibrium distributions obtained for enzyme in the absence and presence of sucrose (0.5 M), the lactate dehydrogenase is essentially dimeric in both environments. The observed stabilization of enzyme activity has therefore been considered in terms of the space-filling effects of sucrose on an isomerization equilibrium between native and unfolded forms of dimeric lactate dehydrogenase, which precedes irreversible inactivation of the unfolded isomer. Interpretation of the kinetic results on that basis has led to the conclusion that the initial stage of enzyme unfolding entails a minor change in volume and/or asymmetry of the lactate dehydrogenase that gives rise to a 4% increase in the second virial coefficient describing excluded volume interactions between dimeric enzyme and sucrose.
Keyword Excluded volume
Lactate dehydrogenase
Molecular crowding
Protein stablization
Thermodynamic nonideality
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
Versions
Version Filter Type
Citation counts: Scopus Citation Count Cited 31 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sat, 09 Jul 2016, 17:29:47 EST by System User