Abstract
Inhibition of the novel oligopeptidase B from Serratia proteamaculans (PSP) by basic pancreatic trypsin inhibitor, Zn2+ ions, and o- and m-phenanthroline was investigated. A pronounced effect of calcium ions on the interaction of PSP with inhibitors was demonstrated. Inversion voltamperometry and atomic absorption spectrometry revealed no zinc ions in the PSP molecule. Hydrophobic nature of the enzyme inhibition by o- and m-phenanthroline was established.
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Abbreviations
- AAS:
-
atomic absorption spectroscopy
- BAPNA:
-
Nα-benzoyl-DL-arginine-p-nitroanilide
- BPTI:
-
bovine basic pancreatic trypsin inhibitor
- buffer A:
-
0.1 M Tris-HCl (pH 8.0)
- DMSO:
-
dimethyl sulfoxide
- IVA:
-
inversion voltamperometry
- OpdB:
-
oligopeptidase B
- PSP:
-
proteinase from Serratia proteamaculans
- p-NA:
-
p-nitroanilide
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Original Russian Text © A. G. Mikhailova, R. F. Khairullin, G. Ya. Kolomijtseva, L. D. Rumsh, 2012, published in Biokhimiya, 2012, Vol. 77, No. 3, pp. 384–391.
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Mikhailova, A.G., Khairullin, R.F., Kolomijtseva, G.Y. et al. Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors. Biochemistry Moscow 77, 300–306 (2012). https://doi.org/10.1134/S0006297912030091
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DOI: https://doi.org/10.1134/S0006297912030091