α-ラクトアルブミン from bovine milk

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.

α-Lactalbumin from bovine milk is suitable for use:

• as an electrophoresis marker, with a molar mass of approximately 14,200Da
• in a study to investigate selective binding of proteins on charged surface iron oxide nanoparticles via reverse charge parity model

α-Lactalbumin was used in the reduction of the antigenicity of whey proteins by lactic acid fermentation.

ガラクトシルトランスフェラ-ゼの基質特異性を変化させてラクト-ス生成速度を上昇させます。ガラクトシルトランスフェラ-ゼとα-ラクトアルブミンの複合体はラクト-スシンタ-ゼとして知られています。

ガラクトシルトランスフェラーゼの基質特異性を変化させてラクトース生成速度を上昇させます。ガラクトシルトランスフェラーゼとα-ラクトアルブミンの複合体はラクトースシンターゼとして知られています。Asp⁸⁷またはAsp⁸⁸のAlaへの部位特異的突然変異誘発は、強力なカルシウム結合親和性を完全に無効にし、ラクトースシンターゼの刺激を最大速度の3.5%未満に低下させます。

α-Lactalbumin 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 a-helices and a triple stranded antiparallel β-sheet.