On the Equilibrium between Monomeric α-Lactalbumin and the Chaperoning Complex of α-Crystallin
| Autor: | Rachel Neal, Frederick A. Bettelheim, J. Samuel Zigler |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Protein Denaturation
animal structures Light Kinetics Biophysics Biochemistry chemistry.chemical_compound Dynamic light scattering Crystallin Lens Crystalline Animals Scattering Radiation Molecular Biology Chromatography High Pressure Liquid Lactalbumin Gel electrophoresis Cell Biology Crystallins Dithiothreitol Crystallography Monomer chemistry Cattle Electrophoresis Polyacrylamide Gel Muramidase Molecular Chaperones |
| Zdroj: | Biochemical and Biophysical Research Communications. 280:14-18 |
| ISSN: | 0006-291X |
| Popis: | In chaperoning dithiothreitol-denatured alpha-lactabumin, alpha-crystallin forms a chaperoning complex. In order to study the kinetics of such chaperoning it needs to be established whether the formation of the chaperoning complex is a reversible or irreversible process. The chaperoning reaction was studied by dynamic light scattering as a function of concentration and weight ratio of alpha-lactalbumin/alpha-crystallin. HPLC and subsequent SDS-PAGE gel electrophoresis experiments established that the chaperoning complex formed contains both alpha-crystallin and alpha-lactalbumin. Upon rechromatographing the chaperoning complex, the presence of monomeric alpha-lactalbumin has been demonstrated in addition to the chaperoning complex itself. This and equilibrium dialysis experiments demonstrated conclusively the existence of an equilibrium between monomeric partially denatured alpha-lactalbumin and the chaperoning complex made of alpha-lactalbumin and alpha-crystallin. |
| Databáze: | OpenAIRE |
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