Project/Area Number |
16570129
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
|
Research Institution | Hokkaido University |
Principal Investigator |
DEMURA Makoto Hokkaido Univ., Fac. of Adv. Life Sci., Prof, 大学院先端生命科学研究院, 教授 (70188704)
|
Co-Investigator(Kenkyū-buntansha) |
AIZAWA Tomoyasu Hokkaido Univ., Fac. of Adv. Life Sci., Associate Prof, 大学院先端生命科学研究院, 助教授 (40333596)
KAWANO Keiichi Hokkaido Univ., Fac. of Sci., Prof, 大学院理学研究院, 教授 (10136492)
NITTA Katsutoshi Hokkaido Univ., Honorary Prof, 名誉教授 (80001858)
|
Project Period (FY) |
2004 – 2006
|
Project Status |
Completed (Fiscal Year 2006)
|
Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2006: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2005: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2004: ¥1,900,000 (Direct Cost: ¥1,900,000)
|
Keywords | apoptosis / protein / oleic acid / NMR / 脂肪酸 / αラクトアルブミン / キメラ |
Research Abstract |
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.
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