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.
D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism*; D003459:Crystallins / Q000378:metabolism*; D007908:Lens, Crystalline / Q000378:metabolism*; D011132:Polyribosomes / Q000378:metabolism; D012995:Solubility; D014508:Urea
D003459:Crystallins; D014508:Urea