Klappa, Peter and Bass, Rosemary and Ruddock, Lloyd W. and 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. (The full text of this publication is not available from this repository)
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.
|Subjects:||Q Science > Q Science (General)|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Peter Klappa|
|Date Deposited:||04 Sep 2008 15:08|
|Last Modified:||24 Jun 2014 10:59|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/3963 (The current URI for this page, for reference purposes)|