Transglutaminase-catalyzed crosslinking of the Aalpha and gamma constituent chains in fibrinogen.

@article{Murthy2000TransglutaminasecatalyzedCO,
  title={Transglutaminase-catalyzed crosslinking of the Aalpha and gamma constituent chains in fibrinogen.},
  author={Subramanyam N. Murthy and James H. Wilson and T. J. Lukas and Yuri I. Veklich and John W. Weisel and Laszlo Lorand},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 1},
  pages={44-8}
}
Studies on transglutaminases usually focus on the polymerization of protein substrates by intermolecular N(epsilon)(gamma-glutamyl)lysine bridges, without considering the possibility that the monomeric protein units, themselves, could also become crosslinked internally. Both types of crosslinks are produced in the reaction of fibrinogen with red cell transglutaminase. We isolated the transglutaminase-modified, mostly monomeric form (92-96%) of fibrinogen with a N(epsilon)(gamma-glutamyl)lysine… CONTINUE READING