|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Agriculture / Faculty of Agriculture >
Peer-reviewed Journal Articles, etc >
Specific inhibitor and substrate specificity of alkaline phosphatase expressed in the symbiotic phase of the arbuscular mycorrhizal fungus, Glomus etunicatum
| Title: | Specific inhibitor and substrate specificity of alkaline phosphatase expressed in the symbiotic phase of the arbuscular mycorrhizal fungus, Glomus etunicatum |
| Authors: | Ezawa, Tatsuhiro Browse this author →KAKEN DB | | Kuwahara, Shin-ya Browse this author | | Sakamoto, Kazunori Browse this author | | Yoshida, Tomio Browse this author | | Saito, Masanori Browse this author |
| Keywords: | beryllium | | enzyme | | sugar phosphate |
| Issue Date: | Jul-1999 |
| Publisher: | The Mycological Society of America |
| Journal Title: | Mycologia |
| Volume: | 91 |
| Issue: | 4 |
| Start Page: | 636 |
| End Page: | 641 |
| Publisher DOI: | 10.2307/3761249 |
| Abstract: | Specific inhibitor and substrate specificity of alkaline phosphatase in the arbuscule of Glomus etunicatum were investigated, and the possible role of this enzyme in the symbiosis was discussed. Mycorrhizal roots of marigold (Tagetes patula) were digested by cellulase and pectinase to separate the intraradical hyphae from the root tissue, and phosphatase activity was stained at pH 8.5 and 5.0. The activity of alkaline phosphatase (pH 8.5) in arbuscules was inhibited in the presence of beryllium, whereas that of acid phosphatase (pH 5.0) was less sensitive to beryllium. Specificity and effectiveness of beryllium on the alkaline phosphatase was further confirmed using fractionated (soluble and insoluble) enzyme prepared from the separated hyphae. The soluble and insoluble alkaline phosphatases hydrolyzed phosphomonoester compounds (glucose-6-phosphate, β-glycerophosphate, trehalose-6-phosphate and glucose 1-phosphate) but not pyrophosphate compounds (ATP and polyphosphate) which were hydrolyzed by acid phosphatase efficiently. The insoluble alkaline phosphatase showed high specific activity (on a protein basis) and high sensitivity to beryllium. Kinetic analysis of the insoluble alkaline phosphatase suggested the involvement of this enzyme in the sugar metabolism of the fungus due to lower Km values for sugar phosphate such as glucose-6-phosphate and trehalose-6-phosphate. |
| Rights: | © 1999 The Mycological Society of America |
| Type: | article |
| URI: | http://hdl.handle.net/2115/38843 |
| Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 江澤 辰広
|
