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Iron-dependent Binding of Bovine Milk α-casein With Holo-Lactoferrin, but Not Holo-Transferrin

Iron-dependent Binding of Bovine Milk α-casein With Holo-Lactoferrin, but Not Holo-Transferrin

Naoko Shibuya, Yasunaga Yoshikawa, Kiyotaka Watanabe, Hiromichi Ohtsuka, Koichi Orino

Biometals. 2012 Oct;25(5):1083-8.

PMID: 22824971

Abstract:

Bovine milk α-casein has been identified as an iron- and heme-binding protein. However, the physiological role of its iron-binding remains to be elucidated in more detail. α-Casein was immobilized on CNBr-activated Sepharose 4B beads, and the α-casein agarose beads efficiently bound hemin as well as ferrous ammonium sulfate (Fe(2+)) as compared with control beads. Additionally, α-casein-beads bound bovine holo-lactoferrin (Lf), but not holo-transferrin. Lf caused the release of Fe(2+) which had bound to the α-casein-agarose beads beforehand. These results suggest that bovine α-casein iron-dependently binds holo-bovine Lf more strongly than Fe(2+), and that strong binding between them may play a physiological role in regulating iron homeostasis in the bovine mammary gland.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9000719-C	α-Casein from bovine milk		9000-71-9	Price
IAR42411063	α-Casein−Agarose			Price

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