Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

Limited proteolysis as a powerful tool for probing flexible oligopeptide portions among different classes of glutathione transferases

Simple item page
dc.contributor.authorNuccetelli, Marzia
dc.contributor.authorEvangelisti, Cristina
dc.contributor.authorCapo, Concetta
dc.contributor.authorPetruzzelli, Raffaele
dc.contributor.authorParker, Michael William
dc.contributor.authorBoard, Philip
dc.contributor.authorCaccuri, Anna Maria
dc.contributor.authorFederici, Giorgio
dc.contributor.authorRicci, G
dc.contributor.authorLo Bello, Mario
dc.date.accessioned2015-12-13T23:20:29Z
dc.date.available2015-12-13T23:20:29Z
dc.date.issued2001
dc.date.updated2015-12-12T09:03:19Z
dc.description.abstractWe have probed possible flexible regions of different GSTs by limited proteolysis experiments. The results indicate that each isoenzyme is inactivated by trypsin and protected against this proteolytic attack by glutathione (GSH). Unlike the results previously obtained with glutathione transferases (GST) GST P1-1, the region most susceptible to the cleavage and responsible for the loss of enzymatic activity in GST A1-1 is located at C-terminus (helix 9) whilst GST M2-2 does not show any primary cleavage site. These findings indicate that helix 2 of GST P1-1 and helix 9 of GST A1-1 may perform a class-specific role.
dc.identifier.issn0009-2797
dc.identifier.urihttp://hdl.handle.net/1885/90722
dc.publisherElsevier
dc.sourceChemico-Biological Interactions
dc.subjectKeywords: Enzymatic activity; Flexibility; Glutathione transferase; Limited proteolysis
dc.titleLimited proteolysis as a powerful tool for probing flexible oligopeptide portions among different classes of glutathione transferases
dc.typeJournal article
local.bibliographicCitation.lastpage48
local.bibliographicCitation.startpage43
local.contributor.affiliationNuccetelli, Marzia, Universita di Roma 'Tor Vergata'
local.contributor.affiliationEvangelisti, Cristina, National Institute for Infectious Diseases
local.contributor.affiliationCapo, Concetta, Universita di Roma 'Tor Vergata'
local.contributor.affiliationPetruzzelli, Raffaele, Universita D'Annunzio
local.contributor.affiliationParker, Michael William, St Vincent's Institute, Biota Str Biol Lab
local.contributor.affiliationBoard, Philip, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationCaccuri, Anna Maria, Universita di Roma 'Tor Vergata'
local.contributor.affiliationFederici, Giorgio, Children's Hospital IRCCS
local.contributor.affiliationRicci, G, Children's Hospital IRCCS
local.contributor.affiliationLo Bello, Mario, Universita di Roma 'Tor Vergata'
local.contributor.authoruidBoard, Philip, u7701651
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationMigratedxPub21161
local.identifier.citationvolume133
local.identifier.scopusID2-s2.0-0013029162
local.type.statusPublished Version

Downloads

Collections

ANU Research Publications

DSpace software copyright © 2002-2026 LYRASIS

abcd