On the quaternary structure of high-molecular-weight proteins from the bovine eye lens

Electron micrographs of high (40-S) and very-high-molecular-weight (240S) alpha-crystallin preparations show large aggregates with a random arrangement of individual low-molecular-weight alpha-crystallin molecules. The electron microscopic data are completed with viscosimetric and light-scattering experiments. All data obtained with higher-molecular-weight alpha-crystallins point to aggregates with non-spherical structures.