Purification and characterization of HSP70 proteins from Torpedo electric organ

Jerry Eichler; Nicola Tolliday; Lilly Toker; Israel Silman

doi:10.1016/0305-0491(94)00164-P

Purification and characterization of HSP70 proteins from Torpedo electric organ

Jerry Eichler, Nicola Tolliday, Lilly Toker, Israel Silman

Research output: Contribution to journal › Article › peer-review

Abstract

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 language	English
Pages (from-to)	409-415
Number of pages	7
Journal	Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
Volume	110
Issue number	2
DOIs	https://doi.org/10.1016/0305-0491(94)00164-P
State	Published - 1 Jan 1995
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biochemistry
Physiology
Aquatic Science
Animal Science and Zoology
Molecular Biology

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10.1016/0305-0491(94)00164-P

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abstract = "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.",

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AU - Tolliday, Nicola

AU - Toker, Lilly

AU - Silman, Israel

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AB - 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.

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Purification and characterization of HSP70 proteins from Torpedo electric organ

Abstract

Keywords

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