Project/Area Number |
06680048
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
|
Allocation Type | Single-year Grants |
Research Field |
家政学
|
Research Institution | Mukogawa Women's University |
Principal Investigator |
DOI Hiroshi Mukogawa Women's University, Department of Food Science and Nutrition. Associate Professor, 生活環境学部, 助教授 (50106267)
|
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: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1994: ¥1,400,000 (Direct Cost: ¥1,400,000)
|
Keywords | Microtubule / Tubulin / Barley / Barley Flour / Classification / Cell Funciton / 微小管形成 / GTPase活性 |
Research Abstract |
Barley is one of the major crop produced in the world. The majority of barley produced is used as animal feed. The use of barley is therefore very different from other grain crops. The reason for this is that the grain is much harder than that of rice or wheat. Consequently, the useage of crop is limited with ocnsequent decrease in economic value. Barley is usefull as a foodstuff, because it contains high levels of protein, dietary fibers and minerals. Recently a new method for the milling of barley grain by a tangential scraping action. We have been attampting to isolate biologically active materials from classified barley flour. It is well-known that tubulin exists in eukaryotic cell widely, and that it forms microtubules by self assembly. Microtubules take part in various cell functins. When tubulin forms microtubules, GTPase activity is observed. It means that materials affecting GTPase activity of tubulin take part in the cell functions. In this study, the purification of the material affecting GTPase activity of tubulin is described. The materials was obtained from the classifed barley flour produced in Japan. The 95-75 % classification flour was used as the starting material for the purification. After cold aceton treatment of the flour, water extract was chromatographed on a Sephacryl S-100HR column. The final preparation obtained from DEAE-Sephadex A-50 ion exchange chromatography and Bio-Gel P-4 gel chromatography was a glycoprotein with a molecular weight of 14,500 dalton containing much aspartic acid and glycine.
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