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Analysis of d-β-Aspartyl Isomers at Specific Sites in Proteins

  • Noriko FujiiEmail author
  • Norihiko Fujii
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 794)

Abstract

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 words

d-Amino acid β-Aspartic acid Aging RP-HPLC Mass spectrometry Enantiomer Isomer Lens crystallin 

Notes

Acknowledgment

This work was supported by a grant from the Ministry of Education, Culture, Sports, Science and Technology of Japan.

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Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  1. 1.Research Reactor InstituteKyoto UniversityOsakaJapan

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