Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus.

@article{Chen2001SolutionSO,
  title={Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus.},
  author={C Chen and Chi Hsin Hsu and Nan-Wei Su and Young C. Lin and Shyh Horng Chiou and Shi Hua Wu},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 48},
  pages={45079-87}
}
Bungarus fasciatus fraction IX (BF9), a chymotrypsin inhibitor, consists of 65 amino acid residues with three disulfide bridges. It was isolated from the snake venom of B. fasciatus by ion-exchange chromatography and belongs to the bovine pancreatic trypsin inhibitor (BPTI)-like superfamily. It showed a dissociation constant of 5.8 x 10(-8) m with alpha-chymotrypsin as measured by a BIAcore binding assay system. The isothermal titration calorimetry revealed a 1:1 binding stoichiometry between… CONTINUE READING