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. Author manuscript; available in PMC: 2009 Dec 1.
Published in final edited form as: J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Oct 21;876(1):69–75. doi: 10.1016/j.jchromb.2008.10.022

Table 2.

Models and equations used to fit frontal analysis and zonal elution data

Method & Model [Reference] Equationa
Frontal analysis:
  One-site model [1]
1mLapp=1(KamL[A])+1mL
(1)
  Two-site model [37]
1mLapp=1+Ka1[A]+β2Ka1[A]+β2Ka12[A]2mL{(α1+β2α1β2)Ka1[A]+β2Ka12[A]2}
(2)
lim[A]01mLapp=1mL{(α1+β2α1β2)Ka1[A]+(α1+β22α1β22)mL(α1+β2α1β2)2
(3)
Zonal elution:
 One-site direct competition 4]
1k=KIVM[I]KamL+VMKamL
(4)
 Two-site allosteric effect [38]
k0(k0k)=[1(βIA1)][1+(1KIL[I])]
(5)
a

Symbols: mLapp, moles of applied analyte at the mean point of a breakthrough curve; [A], concentration of applied analyte; mL, total moles of binding sites that bind to A in Eqns. (1)–(3), or moles of sites at which I and A compete in Eqn. (4); Ka1, association equilibrium constant for the highest affinity site for A in a multi-site system; α1, fraction of all binding sites that belong to the high affinity sites for A; β2, ratio of the association equilibrium constants for the low versus high affinity sites in a two-site system; VM, void volume; [I], concentration of competing agent; Ka is the association equilibrium constant for the binding of A to a ligand; KI, association equilibrium constant for I at its site of competition with A; k, retention factor for A; k0, retention factor for A in the absence of I.