Mutual diffusion of crystallin proteins at finite concentrations: A light-scattering study
✍ Scribed by M. Delaye; A. Gromiec
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 996 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Both static and quasielastic light-scattering measurements were performed on solutions of crystallin proteins extracted from calf lens cortex. The concentration range between ideal (c -0) and physiologic solutions (c up to 50%, w/w) was investigated. The intensity data are compatible with a model where the globular crystallins behave as "hard spheres," the radius of which does not depend on concentration. The correlation function of the scattered intensity is correctly described by a single exponential (mutual diffusion) for 0 < c < 5%. For larger concentrations, a slowly relaxing component, whose amplitude increases with c, appears on top of the rapid component describing the mutual diffusion. Heterodyne detection is used to uncouple these two components. The mutual diffusion coefficient is then found to decrease linearly up to c N 10% and to deviate sharply from linearity at larger concentrations.