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Article: Specific inhibition of protein disulphide reductase activity of a 60kda rat liver protein by adenine nucleotides

TitleSpecific inhibition of protein disulphide reductase activity of a 60kda rat liver protein by adenine nucleotides
Authors
Issue Date1998
PublisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/
Citation
Faseb Journal, 1998, v. 12 n. 8, p. A1362 How to Cite?
AbstractA 60 kda protein which catalysed the reduction of DTN'B, 5.5'-dithio-bis(2 nitrobenzoic acid), in an NADPH-dependent manner was purified to single-band homogeneity from rat liver. Amino-terminal sequencing of the first twentyfive amino acids of the protein showed an overall sequence homology of over eighty percent with thioredoxin reductase purified from human placenta. In the presence of thioredoxin obtained either from plant or mammalian origin, the purified protein catalysed the reduction of the interchain disulphides of mouse immunoglobulin G. This protein disulphide reductase activity of the protein was inhibited by millimolar levels of adenosine tri- and di-phosphate in a metallic cation-independent manner. Adenosine monophosphate did not inhibit the reaction. Other nucleotides such as Uridine tri-, di- and monophosphates, Guanosine tri -, di- and monophosphates, Cytosine tri- and monophosphates also did not have any inhibitory effects. None of the above nucleotides affect the enzyme activity of the protein when DTNB was used as the substrate, indicating that both ATP or ADP did not cause an inactivation of catalytic site. Our results suggest that the purified 60kda protien is thioredoxin reductase. This is the first demonstration that both ATP and ADP, which occur in cells at millimolar quantities, can inhibit the protein disulphide reductase activity of the thioredoxin reductase/thioredoxin couple. This may represent a potential regulatory mechanism for the reduction of intracellular protein disulphides.
Persistent Identifierhttp://hdl.handle.net/10722/147549
ISSN
2015 Impact Factor: 5.299
2015 SCImago Journal Rankings: 2.775

 

DC FieldValueLanguage
dc.contributor.authorSiu, FKen_US
dc.contributor.authorLee, Wen_US
dc.contributor.authorJs, Ken_US
dc.contributor.authorWong, NSen_US
dc.date.accessioned2012-05-29T06:04:31Z-
dc.date.available2012-05-29T06:04:31Z-
dc.date.issued1998en_US
dc.identifier.citationFaseb Journal, 1998, v. 12 n. 8, p. A1362en_US
dc.identifier.issn0892-6638en_US
dc.identifier.urihttp://hdl.handle.net/10722/147549-
dc.description.abstractA 60 kda protein which catalysed the reduction of DTN'B, 5.5'-dithio-bis(2 nitrobenzoic acid), in an NADPH-dependent manner was purified to single-band homogeneity from rat liver. Amino-terminal sequencing of the first twentyfive amino acids of the protein showed an overall sequence homology of over eighty percent with thioredoxin reductase purified from human placenta. In the presence of thioredoxin obtained either from plant or mammalian origin, the purified protein catalysed the reduction of the interchain disulphides of mouse immunoglobulin G. This protein disulphide reductase activity of the protein was inhibited by millimolar levels of adenosine tri- and di-phosphate in a metallic cation-independent manner. Adenosine monophosphate did not inhibit the reaction. Other nucleotides such as Uridine tri-, di- and monophosphates, Guanosine tri -, di- and monophosphates, Cytosine tri- and monophosphates also did not have any inhibitory effects. None of the above nucleotides affect the enzyme activity of the protein when DTNB was used as the substrate, indicating that both ATP or ADP did not cause an inactivation of catalytic site. Our results suggest that the purified 60kda protien is thioredoxin reductase. This is the first demonstration that both ATP and ADP, which occur in cells at millimolar quantities, can inhibit the protein disulphide reductase activity of the thioredoxin reductase/thioredoxin couple. This may represent a potential regulatory mechanism for the reduction of intracellular protein disulphides.en_US
dc.languageengen_US
dc.publisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/en_US
dc.relation.ispartofFASEB Journalen_US
dc.titleSpecific inhibition of protein disulphide reductase activity of a 60kda rat liver protein by adenine nucleotidesen_US
dc.typeArticleen_US
dc.identifier.emailWong, NS:nswong@hkucc.hku.hken_US
dc.identifier.authorityWong, NS=rp00340en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-33749115591en_US
dc.identifier.volume12en_US
dc.identifier.issue8en_US
dc.identifier.spageA1362en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridSiu, FK=55195027300en_US
dc.identifier.scopusauthoridLee, W=14633820600en_US
dc.identifier.scopusauthoridJs, K=14633932300en_US
dc.identifier.scopusauthoridWong, NS=7202836641en_US

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