lipid-binding proteins as probes for lipids
Project/Area Number |
15K14512
|
Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
Cell biology
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Research Institution | Chubu University (2017) Nagoya City University (2015-2016) |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
鈴木 美恵子 名古屋市立大学, 大学院システム自然科学研究科, 研究員 (90624700)
|
Project Period (FY) |
2015-04-01 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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Keywords | リン脂質結合タンパク質 / 毒素タンパク質 / コブラ / コブラサイトトキシン / サイトトキシン / リン脂質結合 / リン脂質プローブ / 脂質結合タンパク |
Outline of Final Research Achievements |
96-well microtiter ELISA plates were coated with several kinds of phospholipids(PLs). The PLs on the plates could be digested quantitatively by phospholipase D even in the absence of detergents. Using these plates 3 kinds of Indian Cobra cytotoxins (CTX2, CTX7,and CTX9) were shown to bind tightly with acidic phospholipids such as phosphatidylserine, but not phosphatidylcholine. Mutant CTX7s were obtained as inclusion body by usung E. coli expression system and were subjected to renaturation under several conditions. However, they didn't show hemolytic activity. Their phospholipid-binding activity could not be measured since the EIA for recombinant CTXs was not established.
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Report
(4 results)
Research Products
(2 results)
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[Journal Article] Comparison of the primary structures, cytotoxicities, and affinities to phospholipids of five kinds of cytotoxins from the venom of Indian cobra, Naja naja.2016
Author(s)
Suzuki-Matsubara, M., Athauda, S. B. P., Suzuki, Y., Matsubara, K. and Akihiko Moriyama, A.
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Journal Title
Comparative Biochemistry and Physiology, Part C
Volume: 179
Pages: 158-164
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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