Effects of dithiothreitol on protein activity unrelated to thiol-disulfide exchange: for consideration in the analysis of protein function with Cleland's reagent.

@article{Alliegro2000EffectsOD,
  title={Effects of dithiothreitol on protein activity unrelated to thiol-disulfide exchange: for consideration in the analysis of protein function with Cleland's reagent.},
  author={Mary Anne Alliegro},
  journal={Analytical biochemistry},
  year={2000},
  volume={282 1},
  pages={
          102-6
        }
}
Dithiothreitol (DTT) is widely used to reduce disulfide bonds in the analysis of protein structure and function. However, thiol-disulfide exchange is not the only mechanism whereby DTT can alter protein function. We observe that DTT diminishes the carbohydrate binding activity of a cysteineless mutant of pigpen as well as it inhibits the intact molecule. Lack of inhibition by threitol, a derivative of the four-carbon sugar threose, indicates that the thiol groups of DTT are required for… CONTINUE READING
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