Sugars decrease the thermal denaturation and aggregation of arachin
Authors:
- 1 October 1985
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 26 (4) , 390-399
Abstract
The effect of three sugars D‐xylose, D‐glucose and D‐sucrose (with increasing hydroxyl content) on the thermal denaturation and protein‐protein interactions of arachin at pH 3.6 were studied by various physicochemical techniques. These included gel melting temperature, turbidity, electrophoresis, viscosity, u.v. difference, fluorescence and circular dichroic measurements. Sugars decreased the heat‐induced aggregation of arachin as shown by the gel melting temperature, turbidity and electrophoretic measurements. Arachin became more compact in the presence of sugars as shown by the reduced viscosity, u.v. difference and fluorescence spectral measurements. Far u.v.‐CD spectral measurements suggested that sugars increase the ordered structure. Viscosity and spectral measurements also showed that heating and cooling in the presence of sugars at pH 3.6 decrease the thermal unfolding of arachin. The effectiveness of the sugar to bring about all the described changes increased with its hydroxyl content. The preventive effect of sugars on the thermal denaturation and aggregation of arachin probably arises from their capacity to strengthen the intra‐protein hydrophobic and hydrogen bonding.Keywords
This publication has 25 references indexed in Scilit:
- REVERSIBLE GELATION OF ARACHINInternational Journal of Peptide and Protein Research, 1980
- Critical solution temperatures of liquid mixtures and the hydrophobic effectThe Journal of Physical Chemistry, 1979
- Isolation and some properties of arachin subunits.Agricultural and Biological Chemistry, 1979
- EFFECT OF SUCCINYLATION ON THE OLIGOMERIC STRUCTURE OF ARACHIN*International Journal of Peptide and Protein Research, 1978
- Effects of sugar solutions on the activity coefficients of aromatic amino acids and their N-acetyl ethyl estersThe Journal of Physical Chemistry, 1976
- Circular dichroism of polypeptide and protein conformations. Film studiesBiochemistry, 1970
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969
- Effect of protein denaturation on micelle stabilityThe Journal of Physical Chemistry, 1969
- Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide GelsNature, 1962
- The globulins of the ground nut (Arachis Hypogaea)Biochimica et Biophysica Acta, 1950