In vitro inactivation of plasma α1-proteinase inhibitor by epoxides and 1,2-dihaloethanes

Ghulam Ansari, Jose C. Gan, Brian K. Barton

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The inactivating effects of three epoxides and two dihaloethanes on the proteinase inhibitory activities of α1-proteinase inhibitor, as well as those of the plasma itself, were investigated. All of the three epoxides (styrene oxide, ethylene oxide and propylene oxide), individually, inactivated the elastase inhibitory or trypsin inhibitory activity of proteinase inhibitor, and that of whole plasma. Styrene oxide is the most effective inactivator of either purified α1-proteinase inhibitor or plasma, followed by ethylene oxide and propylene oxide in a decreasing order of potency. The dihaloethanes, 1,2-dichloroethane and 1,2-dibromoethane, also inactivated the proteinase inhibitory activities of α1-proteinase inhibitor with the former being somewhat more effective than the latter. Concomitant modification of the amino group was also observed with these chemicals.

Original languageEnglish (US)
Pages (from-to)537-542
Number of pages6
JournalArchives of Environmental Contamination and Toxicology
Volume17
Issue number4
DOIs
StatePublished - Jul 1988

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Epoxy Compounds
inhibitor
Peptide Hydrolases
styrene oxide
oxide
Plasmas
plasma
Oxides
Ethylene Oxide
ethylene
Propylene
Styrene
Ethylene
Ethylene Dibromide
Pancreatic Elastase
Trypsin
In Vitro Techniques

ASJC Scopus subject areas

  • Toxicology
  • Environmental Chemistry
  • Environmental Science(all)

Cite this

In vitro inactivation of plasma α1-proteinase inhibitor by epoxides and 1,2-dihaloethanes. / Ansari, Ghulam; Gan, Jose C.; Barton, Brian K.

In: Archives of Environmental Contamination and Toxicology, Vol. 17, No. 4, 07.1988, p. 537-542.

Research output: Contribution to journalArticle

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