FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1574567705> ?p ?o ?g. }

• W1574567705 endingPage "1347" @default.
• W1574567705 startingPage "1340" @default.
• W1574567705 abstract "Abstract Thioredoxin from Escherichia coli (a small hydrogen transport protein containing 108 amino acid residues and having in its oxidized form a single disulfide bond) was acylated with citraconic anhydride. Citraconylation of all amino groups resulted in total loss of enzymatic activity with thioredoxin reductase and immunoprecipitin activity with antithioredoxin antibodies; both these activities were fully restored after deblocking of the citraconylated protein by acid treatment. Large enzymatically inactive peptide fragments of thioredoxin were prepared by selective cleavage at Arg-73 and Met-37, respectively, and tested for their antigenic activity with antibodies against native thioredoxin. Thioredoxin-T-(1-73) and thioredoxin-T-(74-108) were separated by Sephadex G-50 chromatography in 50% acetic acid of a deblocked trypsin digest of citraconylated thioredoxin. Thioredoxin-T-(1-73) afforded about 25% of the corresponding immunoprecipitate of native thioredoxin without significant inhibition at antigen excess. Thioredoxin-T-(74-108) gave no immunoprecipitate but was a potent inhibitor of the reaction of thioredoxin and antithioredoxin as measured by turbidity formation. A major antigenic determinant of thioredoxin was present in the COOH-terminal sequence of the molecule. An equimolar mixture of thioredoxin-T-(1-73) and thioredoxin-T-(74-108) showed full immunoprecipitation activity with antithioredoxin and significant enzymatic activity with thioredoxin reductase. Gel chromatography experiments at pH 8 with the peptide mixture showed a main symmetrical peak with elution volume and amino acid composition identical with native thioredoxin. The results strongly suggested reconstitution of these two fragments to a complex, thioredoxin-T', with a conformation similar to native thioredoxin. Reconstitution of a thioredoxin-like structure was also obtained from a mixture of the overlapping fragments thioredoxin-T-(1-73) and thioredoxin-C-(38-108), although these peptides represented more than the 108 amino acid residues of the protein. Previous results showed reconstitution of thioredoxin-C-(1-37) and thioredoxin-C-(38-108) to a complex called thioredoxin-C' (Holmgren, A. (1972) Fed. Eur. Biochem. Soc. Lett. 24, 351-354). Together with the present results, this shows that three different combinations of two larger peptide fragments obtained by cleavage at two permissible sites gives reconstitution of thioredoxin. In each case, at least one of the component peptides showed strong immunochemical activity with antibodies to native thioredoxin, Netion from a tetrameric to a dimeri" @default.
• W1574567705 created "2016-06-24" @default.
• W1574567705 creator A5074897127 @default.
• W1574567705 creator A5079550858 @default.
• W1574567705 date "1975-02-01" @default.
• W1574567705 modified "2023-09-30" @default.
• W1574567705 title "Reconstitution of Escherichia coli thioredoxin from complementing peptide fragments obtained by cleavage at methionine-37 or arginine-73." @default.
• W1574567705 cites W1419481270 @default.
• W1574567705 cites W1492975997 @default.
• W1574567705 cites W1549581599 @default.
• W1574567705 cites W1554521867 @default.
• W1574567705 cites W1556406069 @default.
• W1574567705 cites W1595838029 @default.
• W1574567705 cites W1596592816 @default.
• W1574567705 cites W1601997381 @default.
• W1574567705 cites W1971088785 @default.
• W1574567705 cites W1974399236 @default.
• W1574567705 cites W1984998534 @default.
• W1574567705 cites W1994844950 @default.
• W1574567705 cites W2017470279 @default.
• W1574567705 cites W2031573483 @default.
• W1574567705 cites W2045777307 @default.
• W1574567705 cites W2045841230 @default.
• W1574567705 cites W2051999418 @default.
• W1574567705 cites W2053607140 @default.
• W1574567705 cites W2074779525 @default.
• W1574567705 cites W2077705879 @default.
• W1574567705 cites W2080814652 @default.
• W1574567705 cites W2088925039 @default.
• W1574567705 cites W2120657153 @default.
• W1574567705 cites W2167996960 @default.
• W1574567705 cites W2238037191 @default.
• W1574567705 cites W2269862327 @default.
• W1574567705 cites W2315788934 @default.
• W1574567705 cites W4230872227 @default.
• W1574567705 doi "https://doi.org/10.1016/s0021-9258(19)41819-x" @default.
• W1574567705 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/803502" @default.
• W1574567705 hasPublicationYear "1975" @default.
• W1574567705 type Work @default.
• W1574567705 sameAs 1574567705 @default.
• W1574567705 citedByCount "40" @default.
• W1574567705 countsByYear W15745677052019 @default.
• W1574567705 countsByYear W15745677052021 @default.
• W1574567705 crossrefType "journal-article" @default.
• W1574567705 hasAuthorship W1574567705A5074897127 @default.
• W1574567705 hasAuthorship W1574567705A5079550858 @default.
• W1574567705 hasBestOaLocation W15745677051 @default.
• W1574567705 hasConcept C104317684 @default.
• W1574567705 hasConcept C151730666 @default.
• W1574567705 hasConcept C175156509 @default.
• W1574567705 hasConcept C181199279 @default.
• W1574567705 hasConcept C185592680 @default.
• W1574567705 hasConcept C2777468819 @default.
• W1574567705 hasConcept C2779281246 @default.
• W1574567705 hasConcept C2780912031 @default.
• W1574567705 hasConcept C3623737 @default.
• W1574567705 hasConcept C43369102 @default.
• W1574567705 hasConcept C515207424 @default.
• W1574567705 hasConcept C547475151 @default.
• W1574567705 hasConcept C55493867 @default.
• W1574567705 hasConcept C86803240 @default.
• W1574567705 hasConceptScore W1574567705C104317684 @default.
• W1574567705 hasConceptScore W1574567705C151730666 @default.
• W1574567705 hasConceptScore W1574567705C175156509 @default.
• W1574567705 hasConceptScore W1574567705C181199279 @default.
• W1574567705 hasConceptScore W1574567705C185592680 @default.
• W1574567705 hasConceptScore W1574567705C2777468819 @default.
• W1574567705 hasConceptScore W1574567705C2779281246 @default.
• W1574567705 hasConceptScore W1574567705C2780912031 @default.
• W1574567705 hasConceptScore W1574567705C3623737 @default.
• W1574567705 hasConceptScore W1574567705C43369102 @default.
• W1574567705 hasConceptScore W1574567705C515207424 @default.
• W1574567705 hasConceptScore W1574567705C547475151 @default.
• W1574567705 hasConceptScore W1574567705C55493867 @default.
• W1574567705 hasConceptScore W1574567705C86803240 @default.
• W1574567705 hasIssue "4" @default.
• W1574567705 hasLocation W15745677051 @default.
• W1574567705 hasOpenAccess W1574567705 @default.
• W1574567705 hasPrimaryLocation W15745677051 @default.
• W1574567705 hasRelatedWork W1225836934 @default.
• W1574567705 hasRelatedWork W1890698591 @default.
• W1574567705 hasRelatedWork W1987528376 @default.
• W1574567705 hasRelatedWork W2048934508 @default.
• W1574567705 hasRelatedWork W2055074397 @default.
• W1574567705 hasRelatedWork W2074344464 @default.
• W1574567705 hasRelatedWork W2146852610 @default.
• W1574567705 hasRelatedWork W2408067028 @default.
• W1574567705 hasRelatedWork W2755232403 @default.
• W1574567705 hasRelatedWork W779113361 @default.
• W1574567705 hasVolume "250" @default.
• W1574567705 isParatext "false" @default.
• W1574567705 isRetracted "false" @default.
• W1574567705 magId "1574567705" @default.
• W1574567705 workType "article" @default.