The in vivo phosphorylation sites of bovine αB‐crystallin

Abstract

Phosphate content determinations established that in alpha B-crystallin two phosphate groups can be present in vivo in bovine lenses. Comparison of tryptic digests of phosphorylated and unphosphorylated alpha B chains, revealed the location of the two phosphorylation sites in tryptic peptides T2 and T3. Thermolytic digestion and gas-phase sequencing demonstrated that Ser-19 and Ser-45 are the in vivo phosphorylation sites of bovine alpha B-crystallin. This pattern of phosphorylation differs from the previously reported in vitro obtained results.