Table 1.

Ca2+ association constants (Ka) for α-lactalbumin or HAMLET

Protein	Ka (M−1)	Buffer	Salt	pH	T (K)	Method	Reference
α-lac human	1.8 • 109	2 mM Tris/HCl	—		298	Chelator	This study
α-lac human	8.3 • 106	2 mM Tris/HCl	150 mM		298	Chelator	This study
			NaCl
HAMLET	5.9 • 108	2 mM Tris/HCl	—		298	Chelator	This study
HAMLET	5.3 • 106	2 mM Tris/HCl	150 mM		298	Chelator	This study
			NaCl
D87A-BAMLET	n.d.*	2 mM Tris/HCl	—		298	Chelator	This study
α-lac bovine	4.3 • 108	10 mM Tris/HCl	—	7.5	298	ITC	a
α-lac goat	5.7 • 108	10 mM Tris/HCl	—	7.5	298	ITC	a
α-lac bovine	2.85 • 108	10 mM Tris/HCl	—	8	—	DSC	b
α-lac bovine	4.8 • 107	10 mM Ammoinium Bicarbonate		7.8		EGTA, Fluoroscence	c
α-lac bovine, human	2.0 • 107	H2O	100 mM	7	294	EDTA, 43Ca-NMR	d
			KCl
α-lac bovine	2.7 • 106	20 mM Tris	—	7.5	298	1) Fluorescence 2) Hummel & Dryer method	e,f
α-lac		5 mM Tris, 0.1	—	7.2	298	CD 270 nm	g
1) bovine	1) 2.5 • 108	mM EDTA
2) human	2) 3 • 108
3) goat	3) 2.8 • 108
Bovine	2.0 • 107	H2O	100 mM KCl	8	294–298	EGTA 13C-NMR	h
Bovine	1) 2.0 • 107	50 mM Hepes	—	8	1) 310	Fluorescence	i
	2) 4.0 • 108				2) 293
Bovine	2.5 • 106	20 mM Tris	—	7.5	298	Microcalorimetry	j

^aVanhooren et al. 2002; ^bHendrix et al. 2000; ^cAnderson et al. 1997; ^dAramini et al. 1992; ^eKronman et al. 1981; ^fBratcher and Kronman 1984; ^gSegawa and Sugai 1983; ^hGerken and Dearborn 1984; ⁱPermyakov et al. 1981; ^jSchaer et al. 1985.