The Binding of Calcium Ions to Bovine Factor X by Rate Dialysis

Summary

The binding of Ca⁺² to bovine factor X (molecular weight of 74,000) (Yue und Gertler 1977) was studied by the technique of rate dialysis and with the use of ⁴⁵Ca⁺². The binding data are consistent with a model of sequential mechanism. One mole of Ca⁺² binds to the glycoprotein with a dissociation constant of 5.2 × 10^-5 M and an additional 39 ± 4 moles of Ca⁺² bind to this zymogen with a dissociation constant of 3.7 × 10^-3M. The binding of the high affinity Ca⁺² causes a functionally significant change in the zymogen, and (calcium) (factor X) complex is the real substrate in the activation process by the protease in Russell’s viper venom.

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