Enzyme activity after resealing within ghost erythrocyte cells, and protection by alpha-crystallin against fructose-induced inactivation.

The role of alpha-crystallin as a molecular chaperone has been shown in many in vitro studies. In the present paper, we report on the chaperone function of alpha-crystallin within resealed erythrocyte ghosts. Eight enzymes were individually resealed within erythrocyte ghosts and assayed at zero time and at 24 h. The ghost cell suspension was separated into soluble and membrane fractions. Five of the enzymes had significantly greater enzyme activity after 24 h than the control within the soluble fractions. Fructation caused a decrease in enzyme activity (relative to the control). Resealing of alpha-crystallin within the ghost cell alongside the enzymes protected against inactivation by fructose within the soluble fraction.