Analysis of d-β-Aspartyl Isomers at Specific Sites in Proteins
Recent studies have shown that biologically uncommon d-β-aspartic acid residues accumulate in specific proteins during the aging process. However, aspartyl residues are not racemized uniformly because d-Asp appears to be confined to particular sites in these proteins. We here describe the method to identify the specific sites of d-β-aspartic acids inversion in proteins.
Key wordsd-Amino acid β-Aspartic acid Aging RP-HPLC Mass spectrometry Enantiomer Isomer Lens crystallin
This work was supported by a grant from the Ministry of Education, Culture, Sports, Science and Technology of Japan.