Linked Life Data

1888010

Source:http://linkedlifedata.com/resource/pubmed/id/1888010

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pubmed-article:1888010pubmed:abstractTextThe preparations of N alpha-Fmoc-3-nitro-L-tyrosine and N-Boc-anthranilic acid Dhbt ester and their application to parallel multiple column solid-phase peptide synthesis is described. A series of peptide substrates containing an anthraniloyl group at the amino terminus and a 3-nitrotyrosyl residue close to the carboxyl terminus have been synthesized. The fluorescence of the anthraniloyl group, intramolecularly quenched by the 3-nitrotyrosine, increases with cleavage of peptide bonds situated between the two groups. The quenching mechanism is of the long-range resonance energy transfer type and long peptide substrates were constructed and used for kinetic measurement on subtilisin Carlsberg and pepsin. Complete quenching was observed even with more than 20 A between the centers of the chromophores, and substrates with up to 50 A between the chromophores were synthesized. The importance of long substrates for optimal enzymatic activity was demonstrated.lld:pubmed
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pubmed-article:1888010pubmed:dateRevised2000-12-18lld:pubmed
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pubmed-article:1888010pubmed:articleTitleAnthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsin.lld:pubmed
pubmed-article:1888010pubmed:affiliationCarlsberg Laboratory, Department of Chemistry, Copenhagen, Denmark.lld:pubmed
pubmed-article:1888010pubmed:publicationTypeJournal Articlelld:pubmed
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