GammaGlu-epsilonLys (γ-Glu-ε-Lys) is used to study the functions and processing of endo-epsilon(-gamma-Glu)-Lys isopeptide bonds in biological processes.
Earlier we detected a novel enzymatic activity in salivary gland secretion of the medicinal leech, splitting isopeptide bonds between the glutamine gamma-carboxamide and lysine epsilon-amino group. This activity is due to destabilase. We described its partial amino acid sequence and
European journal of oral sciences, 119 Suppl 1, 50-54 (2012-01-25)
Tuft protein is a material associated with enamel tufts, and resides in dental enamel primarily at the enamel-dentine junction. It is located primarily at prism peripheries and extends in a very attenuated form towards the enamel outer surface. While it
Development (Cambridge, England), 136(11), 1835-1847 (2009-05-01)
Fertilization is accompanied by the construction of an extracellular matrix that protects the new zygote. In sea urchins, this structure is built from glycoproteins residing at the egg surface and in secretory vesicles at the egg cortex. Four enzymatic activities
Transglutaminases catalyze the formation of γ-glutamylamines utilizing glutamyl residues and amine-bearing compounds such as lysyl residues and polyamines. These γ-glutamylamines can be released from proteins by proteases in an intact form. The free γ-glutamylamines can be catabolized to 5-oxo-L-proline and
Destabilase, endo-epsilon-(gamma-Glu)-Lys-isopeptidase, was prepared from the salivary gland secretion of the medicinal leech (Hirudo medicinalis). The secretion prepared by the known method of Rigbi et al. (1987) (secretion-K) lacks the destabilase-characteristic highly specific isopeptidase activity (the D-dimer-monomerizing activity) because of
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