Roles of Phytase and Calmodulin in Plant Gametophyte
| Project/Area Number |
61560107
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
応用生物化学・栄養化学
|
|---|
| Research Institution | Meijo University |
|---|
Principal Investigator |
AKIRA Hara Meijo Uverisity, Faculty of Agricuture, Associate Professor, 農学部, 助教授 (80041648)
|
|---|
| Project Period (FY) |
1986 – 1987
|
| Project Status |
Completed (Fiscal Year 1987)
|
| Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1987: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1986: ¥1,300,000 (Direct Cost: ¥1,300,000)
|
|---|
| Keywords | Inositol phosphate isomers / phytic acid metabolim / Phytase / Phophatases of Pollen / Calmodulin / Calmodulin-binding protein / Ca^<2+>-binding protein / 花粉のカルモジュリン / フィチン酸 / フィチン酸分解酵素 / イノシトール-三リン酸 / 花粉の生化学 / 【Ca^(2+)】受容タンパク質 |
|---|
| Research Abstract |
The author found a new type of phytase from Typha pollen grains. One of the purposes of this project was what is the role of inositol-triphosphate. which is produced specifically by the hydrolysis of phytic acis with the phytase. Form the results of the analysis by NMR by perstorp Carbotec. Co. (Swden) it was found that the isomer is the myo-inositol 1,2,3-triphosphate which is different from myo-inositol 1,4,5-triphosphate known as a second messunger. I concluded that the specificity of phytase does not have a physiologiocal mean, becaus the inositol-triphosphate was hydroyzed by phosphatases existing in pollen grains and not accumulated during cultivation. It is demonstrated by the chromatogfraphy on a column of Cowex that phytic acid is contained in pollen grains. Phytic acid was silightly digested after l-hr culgivation but almost disappeared after 3hr-cultivation, suggesting that phyti acid is utilized for enough elontaion of pollen tube.
On the study of calmodulin, I tries to purify calmodulin from pollen grains of Typha, pinus and Zea. The purified calmodulin showed the almost same specific activity ad judges homogenous but had duplicate bands in the presence of Ca^<2+> ot EGTA. Three kinds of pollen gtrains contained 0.05-0.10 mg/g pollen and the extracts had the protein bands, seemingly calmodulinbinding proteins, showing different mobilities in the presence of Ca^<2+> and EGTa. The extract o Typha pollen grains fractionated by the chromatography on a DEAE-celluose coumn was electrophoressed on a ployacrylamide gel and yielded some bands showing different mobilities in the presence of calmodulin + Ca^<2+> and EGTA. The identification of these protains isd now progressing.
|
Report
(2 results)
Research Products
(5 results)
