LOSS OF THE C-TERMINAL SERINE RESIDUE FROM BOVINE BETA-B-2-CRYSTALLIN

Electrospray mass spectrometric (ES-MS) examination of bovine beta-crystallins showed a significant component corresponding in mass to beta B-2-crystallin less one serine residue. Tryptic digestion, followed by isolation and characterisation of the C-terminal peptide, demonstrated that this new species has arisen by the loss of the C-terminal serine residue. This phenomenon appears to be age-related since no truncation was detected in beta B-2-crystallin from foetal lenses and the proportion of the truncated form, as judged by ES-MS, was lower in beta-crystallin isolated from calf lenses than that from the lenses of 3-year-old animals. This process therefore is similar to a recently reported loss of the C-terminal serine from alpha-A-crystallin, which we have confirmed using ES-MS. Loss of a C-terminal serine from both crystallins may indicate the presence of carboxypeptidase-A-like activity in bovine lenses. ES-MS data provided no evidence for a significant degree of phosphorylation of beta B-2-crystallin.