The in vivo phosphorylation sites of bovine αB‐crystallin

FEBS Letters

Voorter, Christina E.M.²  Bloemendal, Hans²  de Jong, Wilfried W.²  Meyer, Helmut E.¹  Roersma, Eric S.²  de Haard-Hoekman, Willeke A.² 

[1] Institut für Physiologische Chemie, Ruhr-Universität Bochum, D-4630 Bochum, FRG;Department of Biochemistry, Center for Eye Research, University of Nijmegen, PO Box 9101, 6500 HB Nijmegen, The Netherlands

关键词: Phosphorylation;    Lens protein;    Crystallin;    αB;    RP-HPLC;    reversed-phase high-performance liquid chromatography;    TFA trifluoroacetie acid;    HSP;    heat shock protein;    PTH-DTT;    phenylthiohydantoin-dithiothreitol;   

DOI  :  10.1016/0014-5793(89)81491-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphate content determinations established that in αB-crystallin two phosphate groups can be present in vivo in bovine lenses. Comparison of tryptic digests of phosphorylated and unphosphorylated αB 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 αB-crystallin. This pattern of phosphorylation differs from the previously reported in vitro obtained results.

【 授权许可】

Unknown