Interaction of newly synthesized alpha-crystallin with isolated lens plasma membranes.

Translation of lens polyribosomes in a reticulocyte cell-free system results mainly in the synthesis of the water-soluble crystallins. After incubation of the translation products with isolated lens fiber plasma membranes, the newly synthesized alpha-crystallin interacts with this fraction and becomes water-insoluble. Urea extraction of the reisolated plasma membranes shows that part of the polymeric alpha-crystallin, in particular the alpha A chains, becomes urea-insoluble. When the membranes were isolated under conditions that stabilize complex formation with the cytoskeleton, only alpha A2 seems to interact with this complex. In contract, interaction with beta- and gamma-crystallin could not be observed.