Characterization of human ferritin H chain synthetized in Escherichia coli

Sonia Levi, Gianni Cesareni, Paolo Arosio, Rolando Lorenzetti, Marco Soria, Maurizio Sollazzo, Alberto Albertini, Riccardo Cortese

Research output: Contribution to journalArticle

Abstract

We have inserted the coding region of the cDNA for human ferritin H chain into the expression vector pEMBLex2. The plasmid obtained is able to direct the synthesis of the ferritin H chain in Escherichia coli up to a concentration of 15% of total soluble proteins. All expressed subunits are found correctly assembled in the complete ferritin molecule, which can be easily purified. We have shown that the ferritin synthesized in E. coli has an Mr, electrophoretic mobility, and thermal stability similar to natural human isoferritins and is recognized by monoclonal antibodies specific for the H, but not by those for the L human ferritin chains.

Original languageEnglish
Pages (from-to)269-274
Number of pages6
JournalGene
Volume51
Issue number2-3
DOIs
Publication statusPublished - 1987

Keywords

  • chimeric protein
  • expression vector
  • iron proteins
  • monoclonal antibodies
  • mutagenesis
  • Recombinant DNA

ASJC Scopus subject areas

  • Genetics

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  • Cite this

    Levi, S., Cesareni, G., Arosio, P., Lorenzetti, R., Soria, M., Sollazzo, M., Albertini, A., & Cortese, R. (1987). Characterization of human ferritin H chain synthetized in Escherichia coli. Gene, 51(2-3), 269-274. https://doi.org/10.1016/0378-1119(87)90315-5