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.
D000818:Animals; D002417:Cattle; D002845:Chromatography; D003459:Crystallins; D007525:Isoelectric Focusing; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D011487:Protein Conformation; D012542:Scattering, Radiation; D014461:Ultracentrifugation; D014783:Viscosity
D003459:Crystallins; D046911:Macromolecular Substances