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Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors

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An Erratum to this article was published on 16 May 2012

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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Correspondence to A. G. Mikhailova.

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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

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