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A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein.

Klappa, Peter, Bass, Rosemary, Ruddock, Lloyd W., Freedman, Robert B. (2004) A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. Journal of Biological Chemistry, 279 (7). pp. 5257-5262. ISSN 0021-9258. (doi:10.1074/jbc.M304951200) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:3963)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1074/jbc.M304951200

Abstract

The tripeptide glutathione is the most abundant thiol/disulfide component of the eukaryotic cell and is known to be present in the endoplasmic reticulum lumen. Accordingly, the thiol/disulfide redox status of the endoplasmic reticulum lumen is defined by the status of glutathione, and it has been assumed that reduced and oxidized glutathione form the principal redox buffer. We have determined the distribution of glutathione between different chemical states in rat liver microsomes by labeling with the thiol-specific label monobromobimane and subsequent separation by reversed phase high performance liquid chromatography. More than half of the microsomal glutathione was found to be present in mixed disulfides with protein, the remainder being distributed between the reduced and oxidized forms of glutathione in the ratio of 3:1. The high proportion of the total population of glutathione that was found to be in mixed disulfides with protein has significant implications for the redox state and buffering capacity of the endoplasmic reticulum and, hence, for the formation of disulfide bonds in vivo.

Item Type: Article
DOI/Identification number: 10.1074/jbc.M304951200
Subjects: Q Science > Q Science (General)
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Peter Klappa
Date Deposited: 04 Sep 2008 15:08 UTC
Last Modified: 16 Nov 2021 09:42 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/3963 (The current URI for this page, for reference purposes)

University of Kent Author Information

Klappa, Peter.

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Ruddock, Lloyd W..

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