Purification and characterization of HSP70 proteins from Torpedo electric organ

Jerry Eichler, Nicola Tolliday, Lilly Toker, Israel Silman

Research output: Contribution to journalArticlepeer-review


Members of the HSP70 family were purified from electric organ tissue of Torpedo californica by chromatography on an ATP-agarose column. A 70 kDa protein was the major component purified. The identity of this protein as HSP70 was established by Western blotting with monoclonal antibodies raised against purified and recombinant human HSP70. Sequencing of proteolytic fragments revealed that they possessed high sequence homology with a wide spectrum of members of the HSP70 family from bacteria through to humans. Two minor components, which co-purified with the principal 70 kDa band on the ATP-agarose column, may correspond to Torpedo BiP and to the stress-induced version of HSP70.

Original languageEnglish
Pages (from-to)409-415
Number of pages7
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number2
StatePublished - 1 Jan 1995
Externally publishedYes


  • ATP-agarose
  • BiP
  • Chaperone
  • Cholinergic
  • Electric organ
  • HSP70
  • Heat shock proteins
  • Torpedo

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology


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