The conformation formed by the domain after alanine-155 induces inversion of aspartic acid-151 in alpha A-crystallin from aged human lenses.

@article{Fujii1997TheCF,
  title={The conformation formed by the domain after alanine-155 induces inversion of aspartic acid-151 in alpha A-crystallin from aged human lenses.},
  author={Noriko Fujii and Yuko Momose and Motoo Yamasaki and Tohru Yamagaki and Hiroyuki Nakanishi and Takeshi Uemura and Morichika Takita and Noriyuki Ishii},
  journal={Biochemical and biophysical research communications},
  year={1997},
  volume={239 3},
  pages={918-23}
}
A new cleavage site, which is a post-translational modification, was found between residues His-154 and Ala-155 in alpha A-crystallin from the aged human lens. After trypsin digestion of alpha A-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… CONTINUE READING