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Inactivation of human plasma α1-proteinase inhibitor by a metalloproteinase fromserratia marcescens

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
0167-4838
Publisher
Elsevier
Publication Date
Volume
704
Issue
2
Identifiers
DOI: 10.1016/0167-4838(82)90155-8
Keywords
  • α1-Proteinase Inhibitor
  • Metalloproteinase
  • (S. Marcescens)
Disciplines
  • Biology

Abstract

Abstract The interaction of a Serratia marcescens metalloproteinase with human plasma α 1-proteinase inhibitor has been investigated. The enzyme was not inactivated by this inhibitor but, instead, converted the native plasma protein into an inactive form of decreased molecular weight. Amino terminal sequence analysis indicated that the interaction of the inhibitor and enzyme was at the reactive site of the inhibitor, with peptide-bond cleavage resulting in the inactivation. This process may be important in necrotic processes occurring during bacterial infiltration of host tissues.

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