Affinity Chromatography by Jaroslava Turková (Eds.)

By Jaroslava Turková (Eds.)

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Fig. 5B shows the dependences of the percentages of the obtained enzyme on K after a 10-fold wash, when w/v= 1. For K L = lO-’M a very high degree of purification is already achieved (Pf= 2000), while the percentage of the enzyme obtained is also relatively high. 3 Equilibrium model for elution by a competitive inhibitor The second general method for the setting free the enzyme from its complex with a bound affinity ligand consists in washing it out with a solution of a soluble competitive inhibitor.

For example, when a single wash with a relatively large volume has been employed (w/v= lo), Pf increases from 2 to 22. The decrease in the percentage of the enzyme obtained is also dependent on K L . For example, for K L = lO-’M the percentage of the enzyme obtained decreases only negligibly, for K L = 10-4M the recovery at high K L values decreases from 90%t o 8276, and for K L = loA3M it decreases as much as from 83%to 44%. Fig. 5B shows the dependences of the percentages of the obtained enzyme on K after a 10-fold wash, when w/v= 1.

2 Cooperative adsorption column chromatography Fig. 9 shows typical elution profiles of oligoadenylic acid at various temperatures. The elution centre of the peak is shifted and the peak shape is distorted from a Gaussian type by a decrease in temperature from 15 to O°C. These results indicate that the binding of oligoadenylic acid to polyuridylic acid is stabilized by decreasing the temperature. Further, the distorted elution profiles indicate the cooperativity of the binding of oligoadenylic acid to polyuridylic acid.

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