Bouhallab Saïd, Bouglé Dominique
Science et Technologie du lait et de l'oeuf, UMR 1053 INRA-Agrocampus, 35042 Rennes Cedex, France.
Reprod Nutr Dev. 2004 Sep-Oct;44(5):493-8. doi: 10.1051/rnd:2004053.
The biological and physiological activities of milk proteins are partially attributed to several peptides encrypted in the protein molecules. These peptides can be liberated by enzymatic digestion in vitro and in vivo. Among the biologically active molecules, phosphorylated peptides (caseinophosphopeptides, CPP) are known to exert an effect on calcium metabolism but also on other minerals. While the existing discrepancy on the potential role of CPP on calcium availability has not been clarified, the results of our previous studies showed that a purified phosphopeptide (beta(1-25)) exhibits a positive effect on iron bioavailability in vivo. Here we report the main results on the efficiency of beta(1-25) in the absorption and availability of iron as well as on the mechanism involved.
乳蛋白的生物学和生理活性部分归因于蛋白质分子中加密的几种肽。这些肽可通过体外和体内的酶促消化释放出来。在生物活性分子中,磷酸化肽(酪蛋白磷酸肽,CPP)已知不仅对钙代谢有影响,而且对其他矿物质也有影响。虽然关于CPP对钙可用性的潜在作用的现有差异尚未得到澄清,但我们先前的研究结果表明,一种纯化的磷酸肽(β(1-25))在体内对铁的生物利用度具有积极作用。在此,我们报告β(1-25)在铁的吸收和可用性方面的效率以及所涉及机制的主要结果。