Article
The thrombin high-affinity binding site on platelets is a negative regulator of thrombin-induced platelet activation. Structure-function studies using two mutant thrombins, Quick I and Quick II.
Biochemistry - 10 Mar 1992
Leong L, Henriksen R A, Kermode J C, Rittenhouse S E, Tracy P B
Abstract excerpt
To elucidate the thrombin domains required for high-affinity binding and platelet activation, the platelet binding properties of thrombin and two mutant thrombins, thrombin Quick I and Quick II, were compared to their agonist effects in elevating intraplatelet [Ca2+]. In Quick I, a mutation within the fibrinogen binding groove results in decreased clotting and platelet aggregating activities, whereas in Quick II,...
Topics
- Amino Acid Chloromethyl Ketones
- Amino Acid Sequence
- Binding Sites
- Blood Platelets
- Calcium
- Molecular Sequence Data
- Mutation
- Platelet Activation
- Structure-Activity Relationship
- Thrombin