Sedimentation equilibrium in reacting systems. VII. The temperature-dependent self-association of beta-lactoglobulin A at pH 2.46
| Autor: | E.T. Adams, Lih-Heng Tang |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Concentration dependence
Macromolecular Substances Protein Conformation Self association Biophysics Analytical chemistry Lactoglobulins Calorimetry Biochemistry Animals Scattering Radiation Molecular Biology Apparent weight Equilibrium constant Chemistry Homozygote Temperature Hydrogen-Ion Concentration Molecular Weight Milk Virial coefficient Low speed Models Chemical Sedimentation equilibrium Physical chemistry Molar mass distribution Thermodynamics Cattle Ultracentrifugation Mathematics |
| Zdroj: | Archives of biochemistry and biophysics. 157(2) |
| ISSN: | 0003-9861 |
| Popis: | The self-association of β-lactoglobulin A in 0.2 m glycine buffer (pH 2.46 at 23.5 °C) has been studied by low speed sedimentation equilibrium experiments at 11, 16, 20, 25 °C. In all four sets of experiments the concentration dependence of the apparent weight average molecular weight, M wa , was indicative of a nonideal self-association. The association decreased with increasing temperature. Several models to describe the observed self-association were tested, and a monomer-dimer association describes the data best. Values of the association equilibrium constant, K 2 , and the second virial coefficient, BM 1 , are reported at each temperature. Values of the thermodynamic functions, Δ G °, Δ H °, and Δ S °, are also reported for these experiments. |
| Databáze: | OpenAIRE |
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