Mechanism of the inactivation of guinea pig liver transglutaminase by 5,5'-dithiobis-(2-nitrobenzoic acid).

@article{Connellan1969MechanismOT,
  title={Mechanism of the inactivation of guinea pig liver transglutaminase by 5,5'-dithiobis-(2-nitrobenzoic acid).},
  author={Joanna Connellan and John E. Folk},
  journal={The Journal of biological chemistry},
  year={1969},
  volume={244 12},
  pages={3173-81}
}
Reaction of 5,5’-dithiobis(24trobenzoic acid) (DTNB) with transglutaminase in the absence of calcium ion results in losses in the transferase and hydrolysis activities of the enzyme toward the substrate, benzyloxycarbonyl-L-glutaminylglycine (Z-L-glutaminylglycine). These activities are reduced 70 to 100% by reaction with 1 to 1.5 eq of DTNB. The calcium-dependent esterase activity of transglutaminase toward p-nitrophenyl acetate is not lost by this treatment. However, the activator constant of… CONTINUE READING