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Interaction between titanium and phosphoproteins revealed by chromatography column packed with titanium beads

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/79048

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)

Submitter: 久保木 芳徳

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