title: The in vivo phosphorylation sites of bovine alpha B-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.
authors.affiliation: Department of Biochemistry, University of Nijmegen, The Netherlands.
authors.forename: C E
authors.initials: CE
authors.lastname: Voorter
authors.forename: W A
authors.initials: WA
authors.lastname: de Haard-Hoekman
authors.forename: E S
authors.initials: ES
authors.lastname: Roersma
authors.forename: H E
authors.initials: HE
authors.lastname: Meyer
authors.forename: H
authors.initials: H
authors.lastname: Bloemendal
authors.forename: W W
authors.initials: WW
authors.lastname: de Jong
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000378:metabolism*; D007908:Lens, Crystalline / Q000032:analysis; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation
chemical_list: D003459:Crystallins; D010750:Phosphoproteins