Structural studies on beta H-crystallin from bovine eye lens.

Bovine lens beta H-crystallin, isolated at pH 6.7, undergoes reversible dissociation into dimers and an intermediate size of oligomer (peak A) at pH 5.4. Peak A is enriched in the beta B1 subunit but lacks beta B2, whereas beta B2 is a major component of the dimers. A method for isolation of beta B1 from peak A is described. The pH dependence of the dissociation-reassociation suggests that histidines on the surface of the dimers become buried in the assembly of beta H-crystallin. The positions of the four histidines on the surface of the compact domains of each subunit of the beta B2 homodimer are shown. The beta B1-enriched oligomer has a much lower solubility compared with the beta B2 containing beta H-crystallin. It is possible that beta B2 plays a role in solubilizing beta-crystallin aggregates.