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Specific features of enteropeptidase hydrolysis of chimeric proteins at the specific linker (Asp)4Lys depending on the refolding conditions

Russian Journal of Bioorganic Chemistry volume 26, pages 466–473 (2000)Cite this article

Abstract

Refolding from inclusion bodies of chimeric proteins containing the enteropeptidase-specific linker (Asp)4Lys was carried out. It was shown that, depending on the refolding conditions, chimeric proteins function as substrates or inhibitors of the enteropeptidase. The efficiency of the enteropeptidase hydrolysis of chimeric proteins containing the (Asp)4Lys linker may depend not only on the amino acid sequence of the protein binding site for the enzyme but also on the site’s conformation.

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Abbreviations

HAV:

protein of the VP1 region of the hepatitis A virus

HIV:

protease of the human immunodeficiency virus

HIVR :

protease covalently joined with reverse transcriptase of the human immunodeficiency virus

Nfa:

naphthylamide

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Authors and Affiliations

  1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117871, GSP-7 Moscow, Russia

    E. D. Shibanova, A. G. Mikhailova, S. L. Aleksandrov & L. D. Rumsh

Authors
  1. E. D. Shibanova
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  2. A. G. Mikhailova
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  3. S. L. Aleksandrov
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  4. L. D. Rumsh
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Correspondence to E. D. Shibanova.

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Shibanova, E.D., Mikhailova, A.G., Aleksandrov, S.L. et al. Specific features of enteropeptidase hydrolysis of chimeric proteins at the specific linker (Asp)4Lys depending on the refolding conditions. Russ J Bioorg Chem 26, 466–473 (2000). https://doi.org/10.1007/BF02758617

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  • DOI: https://doi.org/10.1007/BF02758617

Key words

  • chimeric proteins
  • folding
  • limited proteolysis
  • enteropeptidase