The in vivo phosphorylation sites of bovine alpha B-crystallin.
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.
Voorter
C E
CE
Department of Biochemistry, University of Nijmegen, The Netherlands.
de Haard-Hoekman
W A
WA
Roersma
E S
ES
Meyer
H E
HE
Bloemendal
H
H
de Jong
W W
WW
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
D003459:Crystallins; D010750:Phosphoproteins