Structural and functional integrity of specificity and catalytic sites of trypsin.

@article{Grf1988StructuralAF,
  title={Structural and functional integrity of specificity and catalytic sites of trypsin.},
  author={L{\'a}szl{\'o} Gr{\'a}f and Gy{\"o}rgy Hegyi and I Lik{\'o} and Jozsef Hepp and K{\'a}lm{\'a}n Medzihradszky and Charles S. Craik and William J. Rutter},
  journal={International journal of peptide and protein research},
  year={1988},
  volume={32 6},
  pages={512-8}
}
The aspartic acid residue at the bottom of the substrate-binding pocket of trypsin was replaced by glutamic acid through site-directed mutagenesis. The wild-type (Asp-189) and mutant (Glu-189) trypsinogens were expressed in E. coli, purified to homogeneity, activated by enterokinase, and tested on a series of fluorogenic tetrapeptide substrates. The… CONTINUE READING