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…
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