Solution Properties of Phycocyanin. IV. Studies of the Self-association Equilibrium of Phycocyanin in a pH 6.8 Solution
- 1 November 1977
- journal article
- Published by Oxford University Press (OUP) in Bulletin of the Chemical Society of Japan
- Vol. 50 (11) , 2892-2895
- https://doi.org/10.1246/bcsj.50.2892
Abstract
The self-association of phycocyanin in a buffer of pH 6.8 with an ionic strength of 0.1 has been studied by sedimentation equilibrium measurements in the temperature range from 5.2 to 25 °C. The self-association of this system increases with a decrease in the temperature. A quantitative evaluation of the experimental data for this system indicates that the type of the association reaction is not a simple mechanism such as a monomer\ightleftharpoonsn-mer, but the discrete monomer\ightleftharpoonstrimer\ightleftharpoonstetramer mechanism is probable. Several thermodynamic quantities, such as the Gibbs free energy change, ΔG°, the enthalpy change, ΔH°, and the entropy change, ΔS°, accompanying the self-association reaction were computed on the basis of the equilibrium constants. From the results, it is considered that the association process is similar to the ordinary crystallization, and that the formation of a tetramer proceeds at a higher concentration than that in which the trimerization reaction is completed.This publication has 8 references indexed in Scilit:
- Solution Properties of Phycocyanin. III. Studies of the Sedimentation Equilibrium of PhycocyaninBulletin of the Chemical Society of Japan, 1975
- Solution Properties of Phycocyanin. II. Studies of the Molecular Shape and Size by Using the Shell ModelBulletin of the Chemical Society of Japan, 1975
- Solution Properties of Phycocyanin. I. Studies of Dissociation-Association by Sedimentation MeasurementBulletin of the Chemical Society of Japan, 1974
- The temperature-dependent self-association of adenosine 5'triphosphate in 0.154 M NaClBiophysical Chemistry, 1974
- Sedimentation equilibrium in reacting systems. VII. The temperature-dependent self-association of β-lactoglobulin A at pH 2.46Archives of Biochemistry and Biophysics, 1973
- Quaternary Structure of ProteinsAnnual Review of Biochemistry, 1970
- Temperature coefficients of protein partial volumesThe Journal of Physical Chemistry, 1968
- Sedimentation Equilibrium in Reacting Systems. III. Evaluation of the Number Average (Mn(c)) Molecular Weight, Equilibrium Constants, and Nonideal Effects*Biochemistry, 1965