Interaction of newly synthesized alpha-crystallin with isolated lens plasma membranes
- PMID: 7353008
- DOI: 10.1016/0005-2736(80)90170-4
Interaction of newly synthesized alpha-crystallin with isolated lens plasma membranes
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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