Nonequivalence of the metal binding sites of conalbumin. Calorimetric and spectrophotometric studies of aluminum binding.
Differential scanning calorimetric experiments show that addition of Al(III) to conalbumin increases its denaturation temperature by 5 degrees, from 60 to 68 degrees. Only one Al(III) bound per conalbumin molecule produces this change in heat stability; additional bound Al(III) does not affect the heat stability. Since Al(III) displaces both Cu(II) bound at the metal binding sites of conalbumin, binding of aluminum takes place at the same metal binding sites. The binding constant for the second Al(III) is at least 100-fold less than that for the binding of the first Al(III), and both are displaced by added iron. The order of increasing heat stability of the metal ion complexes of conalbumin, Cu(II), Al(III), Fe(III), is the order of increasing binding constant for these metal ions.
D000535:Aluminum; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002151:Calorimetry; D002645:Chickens; D003207:Conalbumin; D003300:Copper; D004527:Egg Proteins; D007700:Kinetics; D011485:Protein Binding; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors
D004527:Egg Proteins; D003207:Conalbumin; D003300:Copper; D000535:Aluminum