Membrane structures and functional correlates in the bi-segmented eye lens of the cephalopod.

The cephalopod eye lens is unique because it has evolved as a compound structure with two physiologically distinct segments. However, the detailed ultrastructure of this lens and precise optical role of each segment are far from clear. To help elucidate structure-function relationships in the cephalopod lens, we conducted multiple structural investigations on squid.

X-ray- and neutron-scattering studies of alpha-crystallin and evidence that the target protein sits in the fenestrations of the alpha-crystallin shell.

Purpose: Alpha-crystallin, a ubiquitous molecular chaperone, is found in high concentrations in the lens. Its structure and precise mechanism of action, however, are unknown. The purpose of these experiments was to further the understanding of the chaperone function of alpha-crystallin.

Transparency of the bovine corneal stroma at physiological hydration and its dependence on concentration of the ambient anion.

De-epithelialised and de-endothelialised bovine corneal stromas with a hydration of 3.2 equilibrated at 154 mM NaCl and buffered at pH 7.4 had their optical density (400-750 nm) measured.