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. 2014 Jun;55(6):1033–1043. doi: 10.1194/jlr.M043067

TABLE 1.

Rate and equilibrium constants, as well as thermodynamic parameters (in kJ mol−1), for the interaction of DHE with the lipoproteins at 35°C. The parameters for DHE interaction with lipid vesicles were taken from literature (11) and are also shown.

HDL3 HDL2 LDL VLDL POPC:Chol 1:1 SM:Chol 6:4
kdiff (1010 M−1 s−1) 2.1 2.9 5.6 14 25 25
kdiff (106 s−1) 143 66 16 2.5 0.77 0.77
k+ (106 M−1 s−1) 3.4 ± 1.2 3.0 ± 1.5 4.1 ± 1.2 21 ± 8 64 ± 6 13 ± 1
kin (102 s−1) 234 ± 84 67 ± 34 12 ± 4 3.9 ± 1.5 2.0 ± 0.2 0.40 ± 0.03
k (10−3 s−1) 30 ± 8 25 ± 9 2.5 ± 1.1 1.7 ± 0.9 0.6 ± 0.2 0.07 ± 0.02
KPLx/W (105)a 11 ± 5 4.2 ± 0.9 11 ± 6 12 ± 10 25 ± 8 47 ± 15
ΔH°(partition) 19 ± 9 4 ± 5 −42 ± 13 24 ± 30 −13 ± 10 53 ± 7
ΤΔS°(partition) 54 ± 10 37 ± 5 −6 ± 13 59 ± 30 23 ± 10b 90 ± 7b
ΔH°(insertion)c 130 ± 10 116 ± 14 90 ± 7 95 ± 15 83 ± 7 110 ± 14
ΤΔS°(insertion)c 93 ± 10 79 ± 15 54 ± 7 63 ± 15 53 ± 7 77 ± 15
ΔH°(desorption)c 111 ± 7 111 ± 10 132 ± 9 72 ± 21 95 ± 12 57 ± 16
ΤΔS°(desorption)c 27 ± 7 26 ± 11 41 ± 9 −20 ± 20 1 ± 12 −43 ± 16
a

The partition coefficient between the aqueous phase and the lipid monolayer at the lipoproteins surface was calculated from the respective equilibrium binding constant as previously described (14).

b

This entropy variation is different from the values given in the original reference because it is calculated from the temperature dependence of KP (instead of KLV) to allow comparison between the parameters obtained for binding agents with very distinct sizes.c refers to the thermodynamic parameters of the transition state in the kinetic steps.