Thermodynamics of gallium complexation by human lactoferrin

Biochemistry. 1986 Feb 25;25(4):803-8. doi: 10.1021/bi00352a011.


Equilibrium constants for the successive binding of 2 equiv of Ga3+ to human lactoferrin have been measured by difference ultraviolet spectroscopy in 0.1 M 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid containing 5 mM bicarbonate at pH 7.4 and 25 degrees C. Ethylenediamine-N,N'-diacetic acid was used as the competing chelating agent. Values of the effective binding constants for the stated experimental conditions are log K1 = 21.43 +/- 0.18 and log K2 = 20.57 +/- 0.16. Comparison of these results with literature values for the gallium-transferrin binding constants indicates that lactoferrin binds gallium more strongly by a factor of approximately 90. The ratios of successive binding constants for the two proteins are essentially identical. A linear free energy relationship (LFER) for the complexation of gallium(III) and iron(III) has been prepared and used to estimate an iron(III)-lactoferrin binding constant for pH 7.4. The LFER prediction is compared with thermodynamic data on iron binding at pH 6.4 and gallium binding at pH 7.4. The results indicate that the ratio of iron binding constants for lactoferrin and transferrin is likely in the range of 50-90.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Gallium / metabolism*
  • Humans
  • Kinetics
  • Lactoferrin / metabolism*
  • Lactoglobulins / metabolism*
  • Protein Binding
  • Spectrophotometry, Ultraviolet
  • Thermodynamics


  • Lactoglobulins
  • Gallium
  • Lactoferrin