Interactions of Recombinant Mouse Erythrocyte Transglutaminase with Membrane Skeletal Proteins

@article{Gutirrez2007InteractionsOR,
  title={Interactions of Recombinant Mouse Erythrocyte Transglutaminase with Membrane Skeletal Proteins},
  author={Edgar B Guti{\'e}rrez and Lanping Amy Sung},
  journal={Journal of Membrane Biology},
  year={2007},
  volume={219},
  pages={93-104}
}
Transglutaminases (TGs) are a family of enzymes that catalyze the formation of covalent γ-glutamyl-ε-lysine crosslinks between glutamine (Q) acyl-donors and lysine (K) acyl-acceptors. Here, we report the cDNA cloning of a TG from mouse reticulocytes, its 4.6-kb message size and high-yield synthesis of recombinant TG in yeast cultures. Its activity was assayed by crosslinking the amine of monodansylcadaverine (DC) onto casein and inside-out vesicles of erythrocytes. The latter contain TG… CONTINUE READING
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