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Extra info for Affinity Techniques - Enzyme Purification: Part B
Once dissolved in water it hydrolyzes rapidly (10-15 minutes at pH 4). ~J. K.
The mixture is gently stirred at 50 ° for 2 hours. 0 containing 1 M NaCl, and 500 ml of 1 M NaC1 at 50 °. The coupled sulfanilamide is 550 /zmoles per gram of dry gel according to the nitrogen content as determined by the Kjeldahl method. 3 M sodium carbonate at pH 10 containing 200 mg of protein. The suspension is gently stirred with a magnetic stirrer at room temperature for 2 hours. 5 M NaC1 in which the gel is stored at 5 °. In the case of soybean trypsin inhibitor, the gel contains 12 ~moles per gram of dry conjugate, and the gel is able to adsorb a stoichiometric amount of trypsin which, in a subsequent step, can be quantitatively desorbed.
S may be considered as a chromatographic measure of affinity. S can be decreased by including in the eluent a substance D that will compete with A for the adsorption sites. ~. kr/(1 + kCA + k'CD) (3) At high concentration of the displacer substance, D, S approaches zero and A will be eluted at or very close to V~, which is the volume determined by molecular sieving in the absence of adsorption. It is also possible to choose k'CD so that kCA ~ 1 + k'CD. Under these conditions, S will be independent of the concentration of A, and the latter substance will travel through the bed as a symmetrical zone with the relative retention due to adsorption equal to K,,.