Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface

@article{Okochi2007DesignOA,
  title={Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface},
  author={Norihiko Okochi and Michiko Kato-Murai and Tetsuya Kadonosono and Mitsuyoshi Ueda},
  journal={Applied Microbiology and Biotechnology},
  year={2007},
  volume={77},
  pages={597-603}
}
Lc-WT, the wild-type light chain of antibody, and Lc-Triad, its double mutant with E1D and T27aS designing for the construction of catalytic triad within Asp1, Ser27a, and original His93 residues, were displayed on the cell surface of the protease-deficient yeast strain BJ2168. When each cell suspension was reacted with BODIPY FL casein and seven kinds of peptide-MCA substrates, respectively, a remarkable difference in hydrolytic activities toward Suc-GPLGP-MCA (succinyl-Gly-Pro-Leu-Gly-Pro-MCA… 
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