Simultaneous stereoinversion and isomerization at specific aspartic acid residues in alpha A-crystallin from human lens.

@article{Fujii1994SimultaneousSA,
  title={Simultaneous stereoinversion and isomerization at specific aspartic acid residues in alpha A-crystallin from human lens.},
  author={Noriko Fujii and Kazue Satoh and Kenich Harada and Yoshihiro Ishibashi},
  journal={Journal of biochemistry},
  year={1994},
  volume={116 3},
  pages={
          663-9
        }
}
We characterized the primary structure of alpha A-crystallin from the lens of the human eye by detailed analyses of the amino acid sequence, mass, and stereoisomers, and found the biologically uncommon D- and beta-aspartic acid (Asp) residues in the protein. The stereoconfiguration of the Asp151 and Asp58 residues in alpha A-crystallin from old subjects (mean age: 80 years) was inverted to the D-isomer, and the residues were simultaneously isomerized to beta-aspartyl residues, which may occur… CONTINUE READING
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