PURIFICATION AND CHARACTERIZATION OF HSP70 PROTEINS FROM TORPEDO ELECTRIC ORGAN

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