Mapping of factor XIII solvent accessibility as a function of activation state using chemical modification methods.

@article{Turner2004MappingOF,
  title={Mapping of factor XIII solvent accessibility as a function of activation state using chemical modification methods.},
  author={Brian T Turner and T Michael Sabo and Diana Wilding and Muriel C Maurer},
  journal={Biochemistry},
  year={2004},
  volume={43 30},
  pages={
          9755-65
        }
}
The transglutaminase Factor XIII (FXIII) catalyzes the formation of covalent cross-links between adjacent noncovalently associated fibrin chains in blood coagulation. The resulting covalently cross-linked hard clot is much more mechanically stable and resistant to proteolytic degradation. FXIII is activated by the serine protease thrombin in the presence of calcium ions. Protein modification experiments involving the labeling of cysteine and lysine side chains of the enzyme were performed… CONTINUE READING

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