Elastase-cathepsin G inhibitors eglin b and eglin c differ by a single Tyr----His substitution. A micro-method for the identification of amino-acid substitution.

@article{Chang1985ElastasecathepsinGI,
  title={Elastase-cathepsin G inhibitors eglin b and eglin c differ by a single Tyr----His substitution. A micro-method for the identification of amino-acid substitution.},
  author={J. Y. Chang and Ren{\'e} Knecht and Reinhard Maschler and Ursula Seem{\"u}ller},
  journal={Biological chemistry Hoppe-Seyler},
  year={1985},
  volume={366 3},
  pages={
          281-6
        }
}
The structures of eglin b and eglin c, both potent inhibitors of human neutral granulocytic proteinase elastase and cathepsin G, were compared by micro amino-acid analysis and peptide mapping techniques. Eglin b and eglin c differ by one amino-acid substitution in the middle of the polypeptide chain. Tyrosine residue at position 35 of eglin c was substituted by histidine in eglin b. This amino-acid substitution requires one base exchange (U----C) at the DNA level and apparently does not affect… 
11 Citations

Binding of the recombinant proteinase inhibitor eglin c from leech Hirudo medicinalis to human leukocyte elastase, bovine alpha-chymotrypsin and subtilisin Carlsberg: thermodynamic study.

The effect of pH and temperature on the apparent association equilibrium constant (Ka) for the binding of the recombinant proteinase inhibitor eglin c from leech Hirudo medicinalis to human leukocyte

The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis Structural analysis, subtilisin structure and interface geometry

The crystal and molecular structure of this complex was determined with data that extended to 0.12-nm resolution by a combination of Patterson search methods and isomorphous replacement techniques and the complete subtilisin molecule could be traced without ambiguity in the refined electron density.

X‐ray crystal structure of the bovine α‐chymotrypsin/eglin c complex at 2.6 Å resolution

The crystal structure of the molecular complex formed by bovine α‐chymotrypsin and the recombinant serine proteinase inhibitor eglin c from Hirudo medicinalis has been solved using monoclinic

A complete quantitative N-terminal analysis method.

  • J. Chang
  • Biology, Chemistry
    Analytical biochemistry
  • 1988

Micro-Isolation of Polypeptides Precolumn Labeled with Hydrophobic Chromophore

Two precolumn labeling techniques for micro-isolation of peptides are developed using DABITC labeling and DABIA labeling for selective isolation of cysteine containing peptides.

Inhibitors of human leukocyte elastase.