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Affinity of the aluminium binding protein
The International Journal of Artificial Organs
|March 1, 1986
Summary
Aluminium binds very tightly to serum transferrin, a protein crucial for iron transport. This strong aluminium-transferrin bond may cause anaemia in patients with aluminium toxicity, even with sufficient iron levels.
Area of Science:
- Biochemistry
- Clinical Chemistry
- Toxicology
Background:
- Transferrin is the primary serum protein responsible for iron transport.
- Aluminium intoxication can lead to various health issues, including anaemia.
- The interaction between aluminium and transferrin is not fully understood.
Purpose of the Study:
- To investigate the binding affinity of aluminium to serum transferrin.
- To determine if aluminium-transferrin binding is reversible.
- To explore the potential role of this binding in aluminium-induced anaemia.
Main Methods:
- In vitro ultrafiltration was employed to assess aluminium binding to transferrin.
- Equilibrium dialysis was used to evaluate the dissociation of aluminium from transferrin.
- The effect of desferrioxamine (DFO) on aluminium-transferrin binding was examined.
Main Results:
- Aluminium exhibits a very high affinity for transferrin.
- The binding of aluminium to transferrin is extremely stable and resistant to dissociation.
- Prolonged dialysis and desferrioxamine (DFO) treatment did not significantly reduce aluminium-transferrin binding.
Conclusions:
- Aluminium forms a very tight and persistent complex with serum transferrin.
- This strong binding may interfere with iron transport and contribute to microcytic hypochromic anaemia in aluminium-intoxicated individuals.
- The findings suggest a mechanism for anaemia development in aluminium toxicity independent of iron availability.