Abstract:
:Phage display techniques using random peptide interactions have supported the role of mammalian glutathione transferase (GST) as part of a signalling pathway for both oxidative stress and an apoptosis pathway. Little is known about the interaction of nonmammalian GST with other proteins. GSTs have been implicated in the development of chronic nematode infections by neutralising cytotoxic products arising from host immune initiated reactive oxygen species (ROS) assault. In this study we attached one of the key GSTs expressed in the model nematode Caenorhabditis elegans to an affinity support matrix and directly identified major interacting proteins by two-dimensional electrophoresis and peptide mass fingerprinting before and following oxidative stress. Nematode GST does not appear to be a stand-alone enzyme and interacts with many types of proteins in both normal and ROS stress conditions. Pull-down proteomic presents a flexible, label free, rapid and economical assay without specialised ligand fishing equipment to identify protein binding partners.
journal_name
Proteomicsjournal_title
Proteomicsauthors
Greetham D,Morgan C,Campbell AM,van Rossum AJ,Barrett J,Brophy PMdoi
10.1002/pmic.200300719subject
Has Abstractpub_date
2004-07-01 00:00:00pages
1989-95issue
7eissn
1615-9853issn
1615-9861journal_volume
4pub_type
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