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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2010-8-2
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pubmed:abstractText |
A recombinant hepsin-producing strain of Escherichia coli was obtained and the conditions for hepsin expression in a bacterial system were optimized. To study the physicochemical properties of the enzyme, a procedure for purification of active recombinant hepsin using metal-chelate affinity chromatography and ion-exchange chromatography was developed. The interaction of recombinant hepsin with various peptide substrates is characterized. The dose-dependent inhibition of the recombinant hepsin enzyme activity by anthralin in vitro and an increase in the hepsin enzymatic activity in the presence of resveratrol were revealed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1608-3040
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
866-72
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pubmed:meshHeading |
pubmed-meshheading:20673210-Anthralin,
pubmed-meshheading:20673210-Cell Line, Tumor,
pubmed-meshheading:20673210-Escherichia coli,
pubmed-meshheading:20673210-Gene Expression,
pubmed-meshheading:20673210-Humans,
pubmed-meshheading:20673210-Kinetics,
pubmed-meshheading:20673210-Recombinant Proteins,
pubmed-meshheading:20673210-Serine Endopeptidases,
pubmed-meshheading:20673210-Serine Proteinase Inhibitors,
pubmed-meshheading:20673210-Stilbenes,
pubmed-meshheading:20673210-Substrate Specificity
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pubmed:year |
2010
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pubmed:articleTitle |
Isolation, purification, and study of properties of recombinant hepsin from Escherichia coli.
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pubmed:affiliation |
Lomonosov Moscow State University, Moscow, Russia. araevskaia@gmail.com
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pubmed:publicationType |
Journal Article
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