What is it about?
In trying to find fibrin degrading proteases, non-plasmin proteases such as human leukocyte elastase, cathepsin G and α-chymotrypsin were found in spleen. Subsequently, inhibitors to these non-plasmin protease were investigated. Eglin C was selected as playing an important role. Next, the active site or structure of Eglin C was examined by making various synthetic substances peptide. This article describes the results.
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Why is it important?
Fibrin degradation cannot be explained only by plasmin. Other way by plasmin became enabled to treat abnormal fibrin deposing diseases.
Perspectives
New drugs referring the present results could solve not only atherothrombotic disease but also cancer-associated thromboembolic diseases and corona-associated thromboembolic diseases.
Junichiro Yamamoto
Read the Original
This page is a summary of: Synthesis of a trihexacontapeptide corresponding to the sequence 8-70 of eglin c and studies on the relationship between the structure and the inhibitory activity against human leukocyte elastase, cathepsin G and α-chymotrypsin, FEBS Letters, October 1990, Wiley,
DOI: 10.1016/0014-5793(90)80461-q.
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