Its
reaction with collagen is commonly assumed to involve the
formation of Schiff bases between the two carbonyl ends of GTA
and positively charged amino groups on the surface of the collagen
and offered D-Lysine. Research has indicated the best candidate to
be the -amino group of lysine, hydroxylysine and arginine side
chains of collagen in the protein molecules creating a structure
more stable than other proteins. In process, GTA easily polymerises
by condensation, giving rise to mixtures of elongated species that
can in turn also cross-link intra and intermolecular lysine of
collagen in a nonspecific manner.