Identification of two of the major phosphorylated polypeptides of the bovine lens utilizing a lens cAMP-dependent protein kinase system.
Two of the major in vitro phosphorylated polypeptides of the bovine lens have been identified. Analysis by means of two-dimensional gel electrophoresis (IEF) has demonstrated that the lens phosphorylated 57,000 and 43,000 dalton polypeptides correspond in mobility to purified phosphorylated bovine lens vimentin and chicken gizzard actin, respectively. Purified actin and vimentin were phosphorylated by a partially purified cAMP-dependent protein kinase isolated from the outer cortex water soluble fraction. All detectable bovine lens vimentin isoelectric variants were phosphorylated. In both the lens fiber cell and chicken gizzard actin preparations, the phosphorylated actin isoelectric variants did not correspond in mobility to the major actin isoelectric variant, but were more acidic. Phosphorylation in all preparations occurred at serine residues.
D000199:Actins / Q000378:metabolism; D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000378:metabolism*; D004586:Electrophoresis / Q000379:methods; D007904:Lens Cortex, Crystalline / Q000201:enzymology*; D007908:Lens, Crystalline / Q000201:enzymology*; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D014746:Vimentin / Q000378:metabolism
D000199:Actins; D003459:Crystallins; D010455:Peptides; D014746:Vimentin; D011494:Protein Kinases