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Bacterial expression of human cysteine proteinase inhibitor stefin A.

Authors
  • Fong, D
  • Kartasova, T
  • Sloane, B F
  • Chan, M M
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Oct 23, 1989
Volume
257
Issue
1
Pages
55–58
Identifiers
PMID: 2680606
Source
Medline
License
Unknown

Abstract

Stefin A, a cysteine proteinase inhibitor of the cystatin superfamily, has been found to be most abundant in epidermal cells. In order to determine its cellular function, we have expressed human stefin A in Escherichia coli using plasmid expression vectors under the control of bacteriophage T7 RNA polymerase. The heat-stable, antibody-positive bacterial product was isolated using a papain-Sepharose affinity column and was shown to inhibit two cysteine proteinases, papain and human cathepsin B. Recombinant stefin A may have commercial and therapeutic potential in situations requiring inhibition of cysteine proteinase activities, and in cosmetics, as an ingredient in skin creams.

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