Construction and Characterization of Calcium Responsive Protein Assembling
| Project/Area Number |
06805071
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
生物・生体工学
|
|---|
| Research Institution | Tokyo Institute of Technology |
|---|
Principal Investigator |
KOBATAKE Eiry Tokyo Institute of Technology, Department of Bioengineering, Associate Professor, 生命理工学部, 講師 (00225484)
|
|---|
| Project Period (FY) |
1994 – 1995
|
| Project Status |
Completed (Fiscal Year 1995)
|
| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1995: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1994: ¥1,500,000 (Direct Cost: ¥1,500,000)
|
|---|
| Keywords | Molecular Assembling / Calmodulin / Fusion Protein / LB membrane / Calcium Ion / Glutathione S-Transferase / カルシウム・イオン / 環境応答 / タンパク質集積体 / インテリジェント・デバイス / 刺激応答膜 |
|---|
| Research Abstract |
In this study, some methods were performed for assembling protein molecules. Calmodulin, a calcium ion responsive protein, was conjugated with lipid and subsequently assembled into a monolayr using LB method. The lipid-conjugated calmodulin retains its calcium sensitivity, determined from the changes in the area-pressure isotherm of the monolayer obtained at the air-water interface.
To assemble calmodulin on a solid-phase matrix, a fusion protein consisting of calmodulin and glutathione S-transferase (GST) was produced by gene fusion. The protein had the modulating activity of calmodulin and binding capability to glutathione of GST.Furthermore, calmodulin could be immobilized on a solid-phase matrix through the use of GST moiety which modulating activity was retained. The activity of phosphodiesterase, which is a calmodulin dependent enzyme, was controlled by the immobilized calmodulin with calcium ion, and repeated use of calmodulin was demonstrated.
|
Report
(3 results)
Research Products
(10 results)
