title: In vitro and in vivo phosphorylation of chicken beta B3-crystallin.
abstract: Incubations of chicken lens homogenates with [32P]-ATP revealed the phosphorylation of a 28 kDa protein, and phosphoamino acid analysis of the phosphorylated protein showed the presence of phosphoserine. The protein is present in the beta-crystallin fraction and after purification and partial sequence determination, by way of peptide mapping and subsequent amino acid analyses and Edman degradation, this 28 kDa protein was identified as the beta B3-crystallin subunit, based on its homology with the bovine and rat orthologue. From phosphate content determination it could be concluded that this chicken beta B3 subunit contains in vivo 2 mol phosphate/mol polypeptide.
authors.affiliation: Department of Biochemistry, University of Nijmegen, The Netherlands.
authors.forename: C E
authors.initials: CE
authors.lastname: Voorter
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; D002645:Chickens; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003459:Crystallins / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*
chemical_list: D003459:Crystallins; D000242:Cyclic AMP; D010770:Phosphotransferases