The phosphorylation of bovine and human lens polypeptides.
The phosphorylation of bovine and human lens polypeptides was examined using an in vitro labeling assay with [gamma-32P]-ATP, followed by SDS-PAGE and radioautography. The major protein phosphorylation in all lens preparations was cAMP-dependent. The effect of cAMP could be depressed by monovalent ions. Phosphorylated polypeptides were detected in capsule-epithelial and outer cortical but not inner cortical-nuclear preparations. Differences in phosphorylated polypeptide distributions and molecular weight patterns were observed between bovine capsule-epithelium and outer cortex fiber cells and bovine and human preparations. Human cataractous lens preparations had the same pattern of phosphorylation as human normal lens preparations but with much less 32P incorporation. Major phosphorylated polypeptides in the 100 000 dalton, 60 000 dalton and 43 000 dalton range were detected in both bovine and human preparations. A 32 000 dalton phosphorylated polypeptide appeared exclusively in the bovine capsule-epithelium and a phosphorylated 23 000 dalton polypeptide was detected only in outer cortical preparations.
D000818:Animals; D001345:Autoradiography; D002386:Cataract / Q000378:metabolism; D002417:Cattle; D000242:Cyclic AMP / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D066298:In Vitro Techniques; D007908:Lens, Crystalline / Q000378:metabolism*; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis / Q000378:metabolism*; D010766:Phosphorylation; D012965:Sodium Chloride / Q000494:pharmacology
D010455:Peptides; D012965:Sodium Chloride; D000242:Cyclic AMP