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

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.

authors

Lorand L,Parameswaran KN,Velasco PT

doi

10.1073/pnas.88.1.82

subject

Has Abstract

pub_date

1991-01-01 00:00:00

pages

82-3

issue

1

eissn

0027-8424

issn

1091-6490

journal_volume

88

pub_type

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