Isolation, purification, and study of properties of recombinant hepsin from Escherichia coli
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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.
Key wordshepsin proteolytic activity anthralin inhibition cytotoxicity human prostate adenocarcinoma
- HAI-1 (2)
hepatocyte growth factor activator inhibitor type I (II)
- P1, P2, P3 and P4
are the specific cleavage site residues enumerated from the C- to N-terminus of the peptide
scavenger cysteine-rich receptor domain
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