By Jaroslava Turková (Eds.)
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Hence, eqn. 9 is also applicable to a comparison of different enzymes. 12) Eqn. 1 3) It follows that ( V - Vi)/(V - Vo) is equal t o the ratio of the enzyme-soluble inhibitor complex concentration to the total enzyme concentration. Eqn. 14) If Vi is plotted against ( V - Vi)/[lo], then KIand Vo can be calculated from the slope and the intercept on the ordinate. If Vo and Vare known, then the value of KI for any competitive inhibitor can be obtained from a single chromatographic run in the presence of the corresponding inhibitor.
Acta, 354 (1974) 121-129. , Biochem. Biophys. Res. ,38 (1970) 875-881. J. , Eur. J. , 41 (1974a) 341-345. J. , Eur. J. Biochem.. 42 (1974b) 1-6. H. ,Biopolymers, 1 (1963) 133-143. , Bailon, P. , Advan. Exp. Med. , 42 (1974) 33-42. , Tanabe, S. , Biopolymers, 14 (1975) 33-49. , 34 (1974) 13-30. Porath, J. , in H. L. 95-178. H. , Chromarographia, 4 (1971) 578-581. , Cuatrecasas, P. , J. Bwl. , 246 (1971) 196-200. , Coupek, J. ,Eiochim. Biophys, Acta, 427 (1976) 586-593. 35 Chapter 4 Application of affinity chromatography to the quantitative evaluation of specific complexes Association processes undoubtedly play one of the most important roles in biochemical processes.
16) where A = 410g(l - 4 p ) -k 4Li2(dp) i- p In the case when p is taken as a parameter, the binding isotherm can be obtained. If the excluded volume effect is taken into consideration, the parameter a can be determined as 2, which appears in a factor due to loops in the partition function, 2n~b(j+l)/(j+2)a. 001), the binding isotherm and the column elution profiles were simulated, but rectangular-type elution profiles were obtained because the binding isotherm tends to zero abruptly at some oligomer concentration, so that it reflects the loop entropy effect of two polymer chains.
Affinity Chromatography by Jaroslava Turková (Eds.)
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