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. 1977 Jun 1;163(3):639–641. doi: 10.1042/bj1630639

Inactivation of human alpha 1-proteinase inhibitor by thiol proteinases.

D Johnson, J Travis
PMCID: PMC1164746  PMID: 301739

Abstract

Human plasma alpha1 proteinase inhibitor is the body's principal modulator of serine proteinases (such as those released from phagocytic cells). Cysteine-active-site proteinases, which are not inhibited, have now been found to inactivate this important inhibitor by proteolytic cleavage of a scissile peptide bond. Papain carries out this inactivation catalytically, whereas cathepsin B1 acts stoicheiometrically. Thus thiol proteinases could easily disrupt the delicately regulated balance between serine proteinases and alpha1 proteinase inhibitor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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