| Project/Area Number |
23580475
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Applied molecular and cellular biology
|
|---|
| Research Institution | Kagoshima University |
|---|
Principal Investigator |
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
ISHIBASHI Matsujiro 鹿児島大学, 農学部, 准教授 (20305163)
TOKUNAGA Hiroko 鹿児島大学, 農学部, 技能補佐員 (60381191)
|
|---|
| Project Period (FY) |
2011 – 2013
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
|
|---|
| Keywords | 好塩性蛋白質 / 可溶化 / 高次構造形成 / まき戻り / 凝集耐性 / タグ / 可溶性 / 変性ストレス耐性 / Brevibacillus / scFv / 可溶性タグ / 金属結合タンパク質 / 好塩性酵素 / 好塩性微生物 / 融合蛋白質 |
|---|
| Research Abstract |
Halophilic proteins, acidic proteins with high content of negative charge, can function under high salt conditions without salting-out effects of salts. High solubility and negative charge repulsion make halophilic protein resistant to various stresses which induce denaturaion of protein, and thus, holophilic proteins are highly resistant to denaturation (resistant to irreversible-aggregation). We isolated several genes of halophilic proteins, characterized, and developed tag to construct fusion proteins.
|
