Thrombin temperature dependence

Studies of the salt and temperature dependence of fibrinopep-tide release show that electrostatic interactions allow thrombin to bind at diffusion-controlled rates (De Gristofaro and Di Cera, 1992 Vindigni and Di Gera, 1996). After thrombin is bound, hydrophobic interactions result in a conformational change in this allosteric enzyme, converting it to a faster form with a higher catalytic efficiency (Guinto et al, 1995). 

Thrombin causes platelet aggregation before it causes clotting the effect is temperature dependent. 

Fibrin dot was prepared by adding thrombin to a buffer sdution of fibrinogen. By stretching the dehydrated dot, oriented films of fibrin were formed. Fibrin contains both a-helix and -form structures. The temperature dependence of the d constant obtained for oriented fibrin films is similar to that for coUa m [29]. 

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