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アブストラクト（24巻4号：神奈川歯学）
Japanese
| Title ： | ウシ歯根膜アルカリホスファターゼの精製とその生化学的性質に関する研究 |
|---|---|
| Subtitle ： | 原著 |
| Authors ： | 竹内誠, 鈴木祥井 |
| Authors（kana） ： | |
| Organization ： | 神奈川歯科大学矯正学教室 |
| Journal ： | 神奈川歯学 |
| Volume ： | 24 |
| Number ： | 4 |
| Page ： | 702-715 |
| Year/Month ： | 1990 / 3 |
| Article ： | 原著 |
| Publisher ： | 神奈川歯科大学学会 |
| Abstract ： | <緒言> 矯正学的な歯の移動は, 矯正力による歯周組織の改造という生体反応によって成立する. これは, 主に歯槽骨における圧迫側の骨吸収と牽引側での骨添加によるが, その他の組織, とりわけ歯槽骨とセメント質との間に介在する歯根膜においてもその線維構造の改造現象が生じている. この歯槽骨における組織改造と, 歯根膜における組織改造とがどのように関連し合っているのかについては不明な点が多い. しかし, 歯に強い矯正力が加わった場合, 圧迫側歯根膜は壊死に陥り, それに接した歯槽骨には骨の吸収が認められず, 壊死組織が肉芽組織に置き換えられ, 新たに分化した線維芽細胞によって歯根膜線維の改造がおこるようになって初めて骨の吸収が始まること, また歯根膜を構成する細胞成分として線維芽細胞のほかに骨芽細胞や破骨細胞の存在が認められていること, などを考えあわせると, 歯槽骨の改造と歯根膜の改造が密接な関連を有していることは容易に想像される. |
| Practice ： | 歯科学 |
| Keywords ： | 歯根膜, アルカリホスファターゼ, 糖鎖構造, ホスファチジルイノシトールグリカン |
English
| Title ： | Purification and Characterization of Alkaline Phosphatase Obtained from Bovine Periodontal Ligament |
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| Subtitle ： | |
| Authors ： | Makoto TAKEUCHI, Yoshii Suzuki |
| Authors（kana） ： | |
| Organization ： | Department of Orthodontics, Kanagawa Dental College |
| Journal ： | Kanagawa Shigaku |
| Volume ： | 24 |
| Number ： | 4 |
| Page ： | 702-715 |
| Year/Month ： | 1990 / 3 |
| Article ： | Original article |
| Publisher ： | Kanagawa Odontological Society |
| Abstract ： | [Abstract]: Alkaline phosphatase (ALP) activity has been demonstrated in periodontal ligament (PDL). On the basis of electron microscopic study, distribution of the enzyme in PDL tissue has also been indicated not only as a cell associated activity but also as an extracellular matrix associated activity. This study is concerned with the purification and characterization of the enzyme obtained from bovine PDL tissue. Purification of ALP extracted from the tissue included solubilization with 10 mM Tris-HCl buffer, pH 7.4, containing 0.2 mM MgCl2 and 0.1% Nonidet P-40 and fractionation by sequential chromatograpy utilizing DEAE-sephacel, Sepharose CL-6B and concanavarin A Sepharose 4B. Purity was established by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This was followd by staining for ALP activity first with 2 mM β-naphthyl acid phosphate and 1 mM Fast Blue BB Salt and then the protein with Coomassie Brilliant Blue. SDS-PAGE of the crude enzyme preparations gave a broad band with apparent molecular weight of 110,000-130,000 dalton. ALP activities were separated into two major peaks using Sepharose CL-6B chromatography. The void volume peak showed a purified form of 110,000 dalton ALP (110K ALP) while the second peak contained 120,000-130,000 dalton ALP (120-130 K ALP) and other proteins. Sequentially, 120-130 K ALP was purified by chromatography on concanavarin A Sepharose 4 B. A polyclonal antibody was raised against purified bovine PDL 110K ALP in a rabbit. Immunodiffusion analysis showed that a polyclonal antibody against 110K ALP recognized 120-130K ALP. Analytical affinity chromatography on concanavarin A Sepharose 4B indicated that 110K ALP and 120-130K ALP had distinct affinity to the column which may depend upon the sugar chain structure. Digestion of 110K ALP with phosphatidylinositol-specific phospholipase C affected electrophoretic mobility but 120-130K ALP had no effect. It is suggested that 110K ALP is attached to a cell membrane anchored by a phosphatidylinositol glycan. In conclusion, bovine PDL contains two types of alkaline phosphatase i. e. 110K ALP and 120-130K ALP. Both ALPs are immunologically related although they have different sugar chain moieties. Furthermore, 110K ALP has a membrane anchoring domain. These results suggest that 110K ALP would be localized on the surface of the cell membrane and 120-130K ALP may associated with the extracellular matrix. |
| Practice ： | Dentistry |
| Keywords ： |
