Table 1.

Percent standard deviation-weighted average values for binding and uptake parameters of two site and one site with Hill Coefficient models

		Two Site Modela				One Site plus Hill Coefficient Modela
Assay	Ligand, Temp	Kd1b,c (µg/ml)	Kd2 (µg/ml)	Bm1 (ng/mg cell protein)	Bm2 (ng/mg cell protein)	Khd (µg/ml)	Hill Coef.	Bhm (ng/mg cell protein)
Binding	LDL, 37°C n=6	1.9±0.2	39±4	993±65	2150±51	28±3	0.65±0.02	2755±84
	HDL, 37°C n=3	7.2±3.1	42±12	282±134	762±98	26±2	0.85±0.02	1003±23
	HDL, 4°C n=6	4.0±0.7	61±6	138±16	469±10	54±5	0.70±0.02	748±21
Assay	Ligand, Temp	Km1b,c (µg/ml)	Km2 (µg/ml)	Vm1 (ng/mg cell protein)	Vm2 (ng/mg cell protein)	Khm (µg/ml)	Hill Coef.	Vhm (ng/mg cell protein)
[3H]CE Uptake	LDL, 37°C n=2	3.5±0.6	100±17	1554±198	7905±344	142±28	0.65±0.02	12280±867
	HDL, 37°C n=3	11.9±1.1	33±4	8367±669	8716±222	31±2	0.82±0.02	12801±256

^aThe errors were calculated using the % standard deviation-weighting approach (see Experimental Procedures).

^bAbbreviations: Kd1, Kd2, apparent (37°C) or true equilibrium (4°C) dissociation constants; Bm1, Bm2, apparent (37°C) or true equilibrium (4°C) maximum binding values; K^hd, apparent (37°C) or true equilibrium (4°C) dissociation constant for the one class of site with negative cooperativity model; B^hm, apparent (37°C) or true equilibrium (4°C) maximum binding value; Km1, Km2, Michaelis constants; Vm1 Vm2, maximum lipid uptake rates; K^hm, Michaelis constant for the one class of site with negative cooperativity model; V^hm, maximum lipid uptake rate for the one site with negative cooperativity model; and Hill Coef, Hill coefficient.

^cFor experiments performed at 37°C the binding values represent apparent dissociation constants and maximal binding, as the measurements were not made under equilibrium conditions (see text).