Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa derived from the Mexican leech Haementeria officinalis.

@article{Theunissen1994MutationalAO,
  title={Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa derived from the Mexican leech Haementeria officinalis.},
  author={Henri J. M. Theunissen and R. D. Dijkema and J C Swinkels and T L de Poorter and Paul M. Vink and Theo van Dinther},
  journal={Thrombosis research},
  year={1994},
  volume={75 1},
  pages={41-50}
}
Antistasin is a Factor Xa inhibitor that is present in the salivary glands of the Mexican leech Haementeria officinalis. The antistasin protein consists of 119 amino acids, of which residues 1-55 (domain I) are 56% similar to residues 56-110 (domain II). Of the nine C-terminal amino acids (residues 111-119; domain III), four are positively charged. The reactive site for Factor Xa is located in domain I. In this study we assessed the role of separate domains and of individual amino acids in the… CONTINUE READING