Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants.

@article{Edge1998EngineeredHC,
  title={Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants.},
  author={Michael D. Edge and Cassie Forder and John F. Hennam and I Lee and David William Tonge and Ian M. Hardern and John Edward Fitton and Kay Eckersley and Simon J East and Ann J. Shufflebotham and Daniel Blakey and Alex Slater},
  journal={Protein engineering},
  year={1998},
  volume={11 12},
  pages={
          1229-34
        }
}
Variants of human pancreatic carboxypeptidase B (HCPB), with specificity for hydrolysis of C-terminal glutamic acid and aspartic acid, were prepared by site-directed mutagenesis of the human gene and expressed in the periplasm of Escherichia coli. By changing residues in the lining of the S1' pocket of the enzyme, it was possible to reverse the substrate specificity to give variants able to hydrolyse prior to C-terminal acidic amino acid residues instead of the normal C-terminal basic residues… Expand
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Six monoclonal antibodies have been isolated from mice immunized with synthetic peptide immunogens whose sequences are derived from that of the human c-myc gene product, and all six antibodies recognize immunoblotted p62c- myc. Expand