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PMID: 7038679 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 78 ·No. 12 ·1981-12-00 ·Pages 7483-6

Abrams WR, Weinbaum G, Weissbach L, Weissbach H, Brot N

Abstract

The major serum inhibitor of proteolytic activity, alpha-1-proteinase inhibitor (alpha-1-PI), (or alpha-1-antitrypsin) can be readily inactivated by oxidation [Carp, H. & Janoff, A. (1978) Am. Rev. Resp. Dis. 118, 617-621]. This inactivation appears to be due to the oxidation of a critical methionine(s) in alpha-1-PI that is required for the inhibition of elastase activity. An enzyme from Escherichia coli that reduces methionine sulfoxide residues in protein [Brot, N., Weissbach, L., Werth, J. & Weissbach, H. (1981) Proc. Natl. Acad. Sci. USA 78, 2155-2158] can restore the biological inhibitory activity of canine oxidized alpha-1-PI.

MeSH Terms
Animals Binding Sites Dogs Escherichia coli/enzymology Methionine/metabolism Methionine Sulfoxide Reductases Oxidation-Reduction Oxidoreductases/metabolism Pancreatic Elastase/antagonists & inhibitors Structure-Activity Relationship alpha 1-Antitrypsin/metabolism
Chemicals
alpha 1-Antitrypsin Methionine Oxidoreductases Methionine Sulfoxide Reductases methionine sulfoxide reductase Pancreatic Elastase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Abrams W R
Weinbaum G
Weissbach L
Weissbach H
Brot N
References (19)
19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.78.12.7483
Published
1981-12-00
Pages
7483-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC349292
Subset
IM
Grants
NHLBI NIH HHS · 5P01HL20994 · United States
External Links
PubMed source DOI: 10.1073/pnas.78.12.7483 PMC Full Text View journal details
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