Bacterial expression of human cysteine proteinase inhibitor stefin A.
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.
Fong
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Department of Biological Sciences and Bureau of Biological Research, Rutgers, State University of New Jersey, Piscataway 08855-1059.
Kartasova
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Sloane
B F
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Chan
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MM
D015153:Blotting, Western; D003001:Cloning, Molecular; D055313:Cystatin B; D015891:Cystatins / Q000235:genetics* / Q000302:isolation & purification / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics*; D005822:Genetic Vectors; D006801:Humans; D007700:Kinetics; D010206:Papain / Q000037:antagonists & inhibitors; D010957:Plasmids; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000494:pharmacology; D015183:Restriction Mapping
C524994:CSTB protein, human; D015891:Cystatins; D011994:Recombinant Proteins; D055313:Cystatin B; D010206:Papain