title: Iron-dependent binding of bovine milk α-casein with holo-lactoferrin, but not holo-transferrin.
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.
authors: Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Towada, Aomori, 034-8628, Japan.
authors: Naoko
authors: N
authors: Shibuya
authors: Yasunaga
authors: Y
authors: Yoshikawa
authors: Kiyotaka
authors: K
authors: Watanabe
authors: Hiromichi
authors: H
authors: Ohtsuka
authors: Koichi
authors: K
authors: Orino
mesh_terms: D000818:Animals; D002364:Caseins / Q000378:metabolism*; D002417:Cattle; D006427:Hemin / Q000378:metabolism; D006706:Homeostasis; D066298:In Vitro Techniques; D007501:Iron / Q000378:metabolism*; D007781:Lactoferrin / Q000378:metabolism*; D008892:Milk / Q000378:metabolism; D011485:Protein Binding
chemical_list: D002364:Caseins; D006427:Hemin; D007501:Iron; D007781:Lactoferrin