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. 1980 Feb 15;596(1):57-63.
doi: 10.1016/0005-2736(80)90170-4.

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

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

F C Ramaekers et al. Biochim Biophys Acta. .

Abstract

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.

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