| Title: | Interaction between titanium and phosphoproteins revealed by chromatography column packed with titanium beads |
| Authors: | Kuboki, Yoshinori Browse this author →KAKEN DB |
| Furusawa, Toshitake Browse this author |
| Sato, Masaaki Browse this author |
| Sun, Yongkun Browse this author |
| Unuma, Hidero Browse this author |
| Fujisawa, Ryuichi Browse this author |
| Abe, Shigeaki Browse this author →KAKEN DB |
| Akasaka, Tsukasa Browse this author →KAKEN DB |
| Watari, Fumio Browse this author →KAKEN DB |
| Takita, Hiroko Browse this author →KAKEN DB |
| Sammons, Rachel Browse this author |
| Keywords: | Titanium binding proteins |
| chromatography |
| phosphoprotein |
| caseins |
| phosvitin |
| dentin phosphoprotein |
| Issue Date: | 2012 |
| Publisher: | IOS Press |
| Journal Title: | Bio-Medical Materials and Engineering |
| Volume: | 22 |
| Issue: | 5 |
| Start Page: | 283 |
| End Page: | 288 |
| Publisher DOI: | 10.3233/BME-2012-0718 |
| Abstract: | The biochemical mechanism behind the strong binding between titanium and living bone has not been fully elucidated, in spite of worldwide clinical application of this phenomenon. We hypothesized that one of the core mechanisms may reside in the interaction between certain proteins in the host tissues and the implanted titanium. To verify the interaction between titanium and proteins, we chose the technique of chromatography in that titanium spherical beads (45 μm) were packed into a column to obtain a bed volume of 16×50 mm, which was eluted with phosphate buffered saline (PBS) and a straight gradient system made by using PBS and 25 mM NaOH. Fetal calf serum, albumin, lysozyme, casein, phosvitin and dentin phosphoprotein (phosphophoryn) were applied to the column. Most part of albumin and lysozyme eluted with the breakthrough peak, indicating practically no affinity to titanium. Fetal bovine serum also eluted mostly as the breakthrough peak, but distinct retained peak was observed. On the other hand, α-casein, phosvitin and phosphophoryn exhibited a distinct retained peak separated from the breakthrough peak. We proposed that phosphate groups (phosphoserines) in the major phosphoproteins, α-casein, phosvitin and phosphophoryn may be involved in the binding of these proteins with titanium. |
| Rights: | The final publication is available at IOS Press through http://dx.doi.org/10.3233/BME-2012-0718 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/79048 |
| Appears in Collections: | 環境科学院・地球環境科学研究院 (Graduate School of Environmental Science / Faculty of Environmental Earth Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
歯学院・歯学研究院 (Graduate School of Dental Medicine / Faculty of Dental Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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