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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1991-2-14
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pubmed:abstractText |
The dansyl-conjugated (Dns) peptides Dns-Pro-Gly-Gly-Gln-Gln-Ile-Val and Dns-Ala-Gln-Gln-Ile-Val, patterned on the N-terminal sequence of fibronectin, were synthesized and used for the transglutaminase (protein-glutamine:amine gamma-glutamyltransferase, EC 2.3.2.13)-directed selective blocking of lens proteins that otherwise might participate in donating lysyl side chains in forming N epsilon-(gamma-glutamyl)-lysine cross-linked oligomers and polymers. Labeling profiles with these peptides could be readily visualized by fluorescence as well as by immunoblotting with anti-dansyl antibody. The labeling patterns in rabbit lens homogenates were quite different with the dansylated peptides than those obtained with dansylcadaverine. Use of such glutamine-containing dansylated peptides should clearly aid in identifying, isolating, and sequencing potential donor substrates of transglutaminases in many biological systems.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
82-3
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1670900-Amino Acid Sequence,
pubmed-meshheading:1670900-Animals,
pubmed-meshheading:1670900-Binding Sites,
pubmed-meshheading:1670900-Cross-Linking Reagents,
pubmed-meshheading:1670900-Crystallins,
pubmed-meshheading:1670900-Dansyl Compounds,
pubmed-meshheading:1670900-Fibronectins,
pubmed-meshheading:1670900-Macromolecular Substances,
pubmed-meshheading:1670900-Molecular Sequence Data,
pubmed-meshheading:1670900-Oligopeptides,
pubmed-meshheading:1670900-Rabbits,
pubmed-meshheading:1670900-Transglutaminases
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pubmed:year |
1991
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pubmed:articleTitle |
Sorting-out of acceptor-donor relationships in the transglutaminase-catalyzed cross-linking of crystallins by the enzyme-directed labeling of potential sites.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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