Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

α-Lactalbumin from bovine milk has been used:in indirect enzyme-linked immunosorbent assay (ELISA) and competitive ELISA methodsin binding of Hsp90 and HSJ1b analysisto inhibit the lysozyme CAP-RAST assay

Biochem/physiol Actions

Alters the substrate specificity of galactosyltransferase to increase the rate of lactose formation; the complex of galactosyltransferase and α-lactalbumin is called lactose synthase. Site-directed mutagenesis of Asp⁸⁷ or Asp⁸⁸ to Ala completely abolishes the strong calcium binding affinity and reduces the stimulation of lactose synthase to ﹤3.5% of the maximal rate.

α-Lactalbumin is the cheif protein in human milk. It consists of a single polypeptide chain with 8 cysteines which form disulfide bridges. α-Lactalbumin binds several metal ions, including calcium, which is thought to play a role in the regeneration of native α-lactalbumin from the reduced, denatured form. α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex.The mature protein consists of 123 amino acid residues (14 kD), and it has a three-dimensional structure with 1.7 Angstrom resolution, demonstrating four α-helices and a triple stranded antiparallel β-sheet.

General description

α-Lactalbumin is a small, globular, whey protein that has been found in all milk studied to date. It is a metalloprotein of approximately 14 kDa produced in the mammary glands.

Packaging

100, 500 mg in poly bottle

1 g in poly bottle

Quality

May contain traces of (NH₄)₂SO₄ and sodium phosphate.