Development and structural characteristic of apoptosis-inducing α-lactalbumin

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α-lactalbumin is a calcium binding protein found in mammalian milk. It is known that α-lactalbumin is one of the components of lactose synthase, which catalyzes the final step in lactose biosynthesis in the lactating mammary gland, and the other component of this system is galactosyltransferase (GT). Most of α-lactalbumin, including human, guinea pig, bovine, goat, camel, equine and rabbit proteins, consist of 123 amino acid residues. Native a-lactalbumin has two structural domains: a large α-helical domain and a small β-sheet domain. The structure is stabilized by four disulfide bridges such as lysozyme. α-lactalbumin forms molten globule state (folding intermediates) at low pH or calcium free state. In this study, development and structural characteristics of the apoptosis-inducing α-lactalbumin as a "non-native" and novel biological function were investigated in detail. A simple and useful method for preparation of non-native structure just like the MG-state which have induction activity of tumor-cell death were developed from not only human but also bovine α-lactalbumin.