Phosphorylation of chick lens proteins.

Phosphorylated proteins of the chick lens were identified following incubation of lenses in a medium containing 32P and subsequent analysis by gel electrophoresis. The acidic variant of the vimentin and both subunits of fodrin were phosphorylated, as were the 95 Kd and 49 Kd proteins associated with the beaded-chain filaments. Neither crystallins nor the main intrinsic membrane proteins were phosphorylated. Several low molecular weight phosphoproteins of the epithelial cell were not present in the fiber cells.