Regulation and specificity of the human disulphide catalyst Ero1-La

The formation of disulphide bonds within many proteins, especially those that are secreted, is essential for their correct folding, stability and function. Disulphlde bonds are formed within the lumen of the Endoplasmic Reticulum (ER) in mammalian cells. Protein disulphide isomerase (PDI) oxidises c...

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Bibliographic Details
Main Author:	Baker, Karl
Published:	University of Manchester 2008
Subjects:	572.633
Online Access:	http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.491846

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spelling	ndltd-bl.uk-oai-ethos.bl.uk-4918462015-03-20T05:16:11ZRegulation and specificity of the human disulphide catalyst Ero1-LaBaker, Karl2008The formation of disulphide bonds within many proteins, especially those that are secreted, is essential for their correct folding, stability and function. Disulphlde bonds are formed within the lumen of the Endoplasmic Reticulum (ER) in mammalian cells. Protein disulphide isomerase (PDI) oxidises cysteine residues in substrate proteins, resulting in the insertion of disulphide bonds into the substrate and the reduction of the oxidised PDI active-site. For PDI to act as an oxidase it needs to have its active-site in an oxidised state. The re-oxidation of PDI is thought to be carried out by the actions of endoplasmic reticulum oxidoreductin 1 (Erol). The aim of this project was to purify recombinant Human Erol-La;, determining its ability to oxidise PDI and to carry out a structure/function analysis to understand how Erol-La; is regulated.572.633University of Manchesterhttp://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.491846Electronic Thesis or Dissertation
collection	NDLTD
sources	NDLTD
topic	572.633
spellingShingle	572.633 Baker, Karl Regulation and specificity of the human disulphide catalyst Ero1-La
description	The formation of disulphide bonds within many proteins, especially those that are secreted, is essential for their correct folding, stability and function. Disulphlde bonds are formed within the lumen of the Endoplasmic Reticulum (ER) in mammalian cells. Protein disulphide isomerase (PDI) oxidises cysteine residues in substrate proteins, resulting in the insertion of disulphide bonds into the substrate and the reduction of the oxidised PDI active-site. For PDI to act as an oxidase it needs to have its active-site in an oxidised state. The re-oxidation of PDI is thought to be carried out by the actions of endoplasmic reticulum oxidoreductin 1 (Erol). The aim of this project was to purify recombinant Human Erol-La;, determining its ability to oxidise PDI and to carry out a structure/function analysis to understand how Erol-La; is regulated.
author	Baker, Karl
author_facet	Baker, Karl
author_sort	Baker, Karl
title	Regulation and specificity of the human disulphide catalyst Ero1-La
title_short	Regulation and specificity of the human disulphide catalyst Ero1-La
title_full	Regulation and specificity of the human disulphide catalyst Ero1-La
title_fullStr	Regulation and specificity of the human disulphide catalyst Ero1-La
title_full_unstemmed	Regulation and specificity of the human disulphide catalyst Ero1-La
title_sort	regulation and specificity of the human disulphide catalyst ero1-la
publisher	University of Manchester
publishDate	2008
url	http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.491846
work_keys_str_mv	AT bakerkarl regulationandspecificityofthehumandisulphidecatalystero1la
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Regulation and specificity of the human disulphide catalyst Ero1-La

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