The conformation formed by the domain after Alanine-155 induces inversion of aspartic acid-151 in αA-crystallin from aged human lenses

Noriko Fujii, Yuko Momose, Miyuki Yamasaki, Tohru Yamagaki, Hiroshi Nakanishi, Toshimasa Uemura, Masatoshi Takita, Noriyuki Ishii

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

A new cleavage site, which is a post-translational modification, was found between residues His-154 and Ala-155 in αA-crystallin from the aged human lens. After trypsin digestion of αA-crystallin two peptides that include Asp-151 were obtained and have remarkable differences. That is, the stereo-configuration of the Asp-151 in the normal length peptide was predominately inverted to the D-isomer of β-aspartyl form (D/L of 5.7). However, the stereoconfiguration of the Asp-151 in the cleavage peptide, that lacks the sequence following Ala-155 to the C-terminus, remained predominately in the L-isomer form as indicated by a D/L value of 0.3. The results suggest that the secondary structure in the region of Ala-155 to the C-terminus may constitute a field that causes the inversion of the Asp-151 to the D-isomer form. Since this kind of cleavage was not found in αA-crystallin from young lens, the cleavage between His-154 and Ala-155 is probably the result of aging.

Original languageEnglish
Pages (from-to)918-923
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume239
Issue number3
DOIs
Publication statusPublished - Oct 29 1997

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'The conformation formed by the domain after Alanine-155 induces inversion of aspartic acid-151 in αA-crystallin from aged human lenses'. Together they form a unique fingerprint.

Cite this