M. Hall et K. Soderhall, CRAYFISH ALPHA-MACROGLOBULIN AS A SUBSTRATE FOR TRANSGLUTAMINASES, Comparative biochemistry and physiology. B. Comparative biochemistry, 108(1), 1994, pp. 65-72
Two fluorescent transglutaminase substrates, dansylcadaverine and a da
nsylated peptide (dansyl-Pro-Gly-Gly-Gln-Gln-Ile-Val), were used to de
tect glutamine and lysine, respectively, as putative transglutaminase
cross-linking residues on purified crayfish alpha-macroglobulin. Endog
enous transglutaminase activities, present in the homogenates of crayf
ish haemocytes and crayfish abdominal muscle, incorporated the dansyla
ted peptide into crayfish alpha-macroglobulin, while guinea-pig liver
transglutaminase incorporated both dansylcadaverine and the dansylated
peptide. Methylamine treatment induces a conformational change in the
crayfish alpha-macroglobulin molecule that also affects its propertie
s as a transglutaminase substrate. None of the dansylated probes were
incorporated by the different transglutaminases into methylamine-treat
ed crayfish alpha-macroglobulin.