Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 292, Issue 2, Pages 505-511Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M116.757302
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Funding
- Council of Scientific and Industrial Research, India [37(1603)/13/EMRII, 37(1604)/13/EMRII)]
- National Institutes of Health Intramural Research Program of the NIDDK
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The reversible thermal denaturation of apo alpha-lactalbumin (alpha-LA) and lysozyme was measured in the absence and presence of multiple concentrations of each of seven saccharides (glucose, galactose, fructose, sucrose, trehalose, raffinose, and stachyose) at multiple pH values. It was observed that with increasing pH, the absolute stability of alpha-LA decreased, whereas the stabilizing effect per mole of all saccharides increased, and that the absolute stability of lysozyme increased, whereas the stabilizing effect per mole of all saccharides decreased. All of the data may be accounted for quantitatively by straightforward electrostatic generalization of a previously introduced coarse-grained model for stabilization of proteins by sugars.
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