| Project/Area Number |
62540515
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
植物生理学
|
|---|
| Research Institution | Toho University |
|---|
Principal Investigator |
KUWABARA Tomohiko Toho University, 理学部, 講師 (80153435)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
TAMAKI Makoto Toho University, 理学部, 講師 (00104141)
|
|---|
| Project Period (FY) |
1987 – 1988
|
| Project Status |
Completed (Fiscal Year 1988)
|
| Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1988: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1987: ¥1,200,000 (Direct Cost: ¥1,200,000)
|
|---|
| Keywords | Protease / Thylakoid / Membrane / Photosystem II / Extrinsic protein / ホウレンソウ / 光化学系II / チラコイド膜 / 光化学系II粒子 / 葉緑体 |
|---|
| Research Abstract |
This work calrified followings: (1) More than one proteases are extrinsically associated with spinach PSII membranes. (2) One protease cleaves a Phe-Gly bond in the 23-KDa protein of PSII water-oxidation complex, and is sensitive to SH-reagents. (3) Another protease is likely to be a prolyl endopeptidase (E.C.3.4.21.26), since a pro-Ile and a Pro Leu bonds in the 18-KDa protein of PSII water-oxidation complex were cleaved. The protease seems to be a new type, since inhibitors specific to prolyl endopeptidases, diisopropyl fluorophosphate and N-benzyloxycarbony1-L- thioproly1-thiazolidine, were ineffective.
An extrinsic protease was purified from spinach PSII membranes by hydrophobic, anion-exchange and gel filtration chromatography. Protease activity was best assayed using the 18-KDa protein as the substrate. Upon gel filtration chromatography, the protease exhibited two peaks at 156 KDa and 39 KDa. Both peaks showed a polypeptide of 39 KDa on SDS-PAGE. Re-chromatography of either peak gave birth to the both of the two peaks. These results suggest that the protease forms a tetramer with the 39-KDa subunit.
|
