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Isolation and partial characterization of the Asp-B10, Tyr-B25-des-(B26-B30)-proinsulin analog from inclusion bodies in Escherichia coli

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Biotechnology Techniques

Summary

A proinsulin analog constructed by site-directed mutagenesis was expressed as a fusion protein that formed inclusion bodies inside the cells. It was purified from the isolated inclusion bodies and proinsulin was obtained by trifluoro-acetic acid, dimethyl sulfoxide and hydrochloric acid cleavage. The released proinsulin analog was confirmed by its molecular weight as determined by SDS-PAGE.

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Authors and Affiliations

  1. Departemento de Biologia Geral, UFMG, Caixa Postal 486, 31270-901, Belo Horizonte, MG, Brazil

    A. M. A. Nascimento

  2. Departamento de Bioquímica e Imunologia, UFMG, Caixa Postal 486, 31270-901, Belo Horizonte, MG, Brazil

    A. M. A. Nascimento & M. Mares-Guia

  3. Biobras S.A, Distrito Industrial, 39.404-004, Montes Claros, MG, Brazil

    H. R. T. Souza, M. S. Xavier, J. E. Thiemann, L. Vilela & M. Mares-Guia

Authors
  1. A. M. A. Nascimento
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  2. H. R. T. Souza
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  3. M. S. Xavier
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  4. J. E. Thiemann
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  5. L. Vilela
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  6. M. Mares-Guia
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Nascimento, A.M.A., Souza, H.R.T., Xavier, M.S. et al. Isolation and partial characterization of the Asp-B10, Tyr-B25-des-(B26-B30)-proinsulin analog from inclusion bodies in Escherichia coli . Biotechnol Tech 10, 737–742 (1996). https://doi.org/10.1007/BF00222558

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  • DOI: https://doi.org/10.1007/BF00222558

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