Changing residue 338 in human factor IX from arginine to alanine causes an increase in catalytic activity.

@article{Chang1998ChangingR3,
  title={Changing residue 338 in human factor IX from arginine to alanine causes an increase in catalytic activity.},
  author={Jufang Chang and Jie Jin and P Lollar and Wolfram Bode and Katharina H{\"a}ussermann and Nobuko Hamaguchi and David L Straight and Darrel W. Stafford},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 20},
  pages={12089-94}
}
This study was designed to identify functionally important factor IX (FIX) residues. Using recombinant techniques and cell culture, we produced a mutant FIX with arginine at 338 changed to alanine (R338A-FIX). This molecule had approximately 3 times greater clotting activity than that of wild type FIX (wt-FIX) in the activated partial thromboplastin assay. R338A-FIX reacted normally with a panel of three FIX specific monoclonal antibodies and migrated on sodium dodecyl sulfate-polyacrylamide… CONTINUE READING

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