Please use this identifier to cite or link to this item:
https://www.um.edu.mt/library/oar/handle/123456789/120712
Title: | GroESL protects superoxide dismutase (SOD)-deficient cells against oxidative stress and is a chaperone for SOD |
Authors: | Hunter, Gary J. Hunter, Therese |
Keywords: | Superoxide dismutase Molecular chaperones Heat shock proteins Oxidative stress |
Issue Date: | 2013 |
Publisher: | SciRes |
Citation: | Hunter, G. J., & Hunter, T. (2013). GroESL protects superoxide dismutase (SOD)—Deficient cells against oxidative stress and is a chaperone for SOD. Health, 5(10), 1719-1729. |
Abstract: | Superoxide dismutase (SOD)-deficient Escherichia coli OX326A cells are protected against chemically-induced oxidative stress by expression of the chaperonin GroESL. This protection is equivalent to expression of superoxide dismutase even though GroESL has no inherent SOD activity. Co-overexpression of GroESL and SOD in the same cells results in higher protein yields of SOD and greater metallation of SOD when compared with expression of SOD alone. Greater metallation results in the higher specific activity of SOD that is observed in heat shock, and is not due to increased synthesis of SOD mRNA or protein. |
URI: | https://www.um.edu.mt/library/oar/handle/123456789/120712 |
Appears in Collections: | Scholarly Works - FacM&SPB |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
GroESL_protects_superoxide_dismutase_SOD_deficient_cells_against_oxidative_stress_and_is_a_chaperone_for_SOD.pdf | 919.79 kB | Adobe PDF | View/Open |
Items in OAR@UM are protected by copyright, with all rights reserved, unless otherwise indicated.