Iron tissue storage and hemoglobin levels of deficient rats repleted with iron bound to the caseinophosphopeptide 1-25 of beta-casein

Caseinophosphopeptides (CPP) issued from enzyme digestion of caseins bind c ations and keep them soluble in the digestive tract. They could be used as ligands to improve iron (Fe) bioavailability. Fe-deficient young rats were repleted with Fe (40 or 200 mg/kg of diet) bound either to the beta-CN (1-2 5) of beta-casein or to whole beta-casein or as FeSO4. A control pair-fed g roup was given 200 mg of Fe (FeSO4)/kg of diet for 6 weeks. After repletion , hemoglobin concentration of the control group was reached only by the bet a-CN (1-25) animals fed 200 mg of Fe/kg; beta-CN (1-25) bound Fe (40 and 20 0 mg) produced higher Fe liver and spleen stores than FeSO4. Binding Fe to the whole, nonhydrolyzed beta-casein gave results intermediate between the other experimental groups. Binding Fe to phosphoserine residues of low mole cular weight CPP improved its ability to cure anemia and to restore iron ti ssue stores, as compared to Fe bound to the whole casein and to inorganic s alts.