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. 1991 Jan 1;88(1):82–83. doi: 10.1073/pnas.88.1.82

Sorting-out of acceptor-donor relationships in the transglutaminase-catalyzed cross-linking of crystallins by the enzyme-directed labeling of potential sites.

L Lorand 1, K N Parameswaran 1, P T Velasco 1
PMCID: PMC50752  PMID: 1670900

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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