Structure and antithrombin-binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela mactroides.

@article{Pejler1987StructureAA,
  title={Structure and antithrombin-binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela mactroides.},
  author={Gunnar Pejler and Anna Danielsson and Ingemar Bj{\"o}rk and Ulf Lindahl and Helena B. Nader and Carl Dietrich},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 24},
  pages={11413-21}
}
Heparin with high anticoagulant activity was isolated from the two marine clam species Anomalocardia brasiliana and Tivela mactroides. A large portion of the polysaccharide chains of both preparations bound with high affinity to immobilized antithrombin. Titrations monitored by tryptophan fluorescence showed that clam polysaccharide chains with Mr approximately 22,500 contained up to three binding sites for antithrombin and that the binding constants for the interaction of these chains with… CONTINUE READING
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