In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites.

@article{Takahashi1995InVG,
  title={In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites.},
  author={Maiko Takahashi and Yun-bi Lu and Tomoko Myint and Junichi Fujii and Yushin Wada and Naoyuki Taniguchi},
  journal={Biochemistry},
  year={1995},
  volume={34 4},
  pages={1433-8}
}
We have reported that the enzyme which reduces 3-deoxyglucosone (3-DG), a major intermediate and a potent cross-linker in the Maillard reaction, is identical with aldehyde reductase [Takahashi, M., Fujii, J., Teshima, T., Suzuki, K., Shiba, T., & Taniguchi, N. (1993) Gene 127, 249-253]. The enzyme purified from normal rat liver was found to be partially glycated as judged by binding to a boronate column and reactivity to anti-epsilon-hexitol lysine IgG. Sites of in vivo glycation of rat liver… CONTINUE READING