アブストラクト（15巻1号：神奈川歯学）

神奈川歯学

Japanese

Title　： ハイドロキシアパタイトに対する骨コラーゲンブロムシアン分解ペプチドの吸着構造
Subtitle　： 原著
Authors　： 小川守
Authors（kana）　：
Organization　： 神奈川歯科大学口腔生化学教室
Journal　： 神奈川歯学
Volume　： 15
Number　： 1
Page　： 51-68
Year/Month　： 1980 / 6
Article　： 原著
Publisher　： 神奈川歯科大学学会
Abstract　： 「緒言」 歯牙, 骨などの硬組織は, ハイドロキシアパタイト(HA)を主要ミネラル成分としている. HAは結晶学的に格子原子の置換, 欠損, および結晶内部の欠陥などにより化学量論的関係は成立しにくいが, 共通のX線回折像をもち, Ca10(PO4)6(OH)2の組成を有していることが明らかにされている. このHA表面には種々なる有機質の吸着現象が証明されており, 特に歯科においてう蝕や歯周疾患の原因の1つと考えられている歯垢形成にHAの構造および結晶表面性質が関与することが知られており, Streptococcus mutans等の菌体外多糖体, および唾液成分のHAへの吸着実験が報告されている. 西山, 斎藤らも人耳下腺唾液を採取し, これを精製した後, HAに吸着させ吸着前と吸着後をdisc電気泳動で比較した結果, 唾液由来のある種のタンパク質が選択的にHAに吸着することを明らかにした.
Practice　： 歯科学
Keywords　：

English

Title　： Adsorbed Structure of Cyanogen Bromide Peptides from Insoluble Bone Collagen by Hydroxyapatite
Subtitle　：
Authors　： Mamoru Ogawa
Authors（kana）　：
Organization　： Department of Oral Biochemistry, Kanagawa Dental College
Journal　： Kanagawa Shigaku
Volume　： 15
Number　： 1
Page　： 51-68
Year/Month　： 1980 / 6
Article　： Original article
Publisher　： Kanagawa Odontological Society
Abstract　： In the field of collagen research, structural approaches on collagen molecules have been remarkably developed lately, and the precise primary structure of collagen was completely established using α1 chain of type I collagen. But more detailed researches were necessary to explain a phenomenon of physiological or pathological calcification in which type I collagen molecules play an important role as predominant mineralizing matrix. It seems reasonable to attempt the experiment to prove the existence of specific structure for collagen which is capable of fit and adsorb to the surface structure of hydroxyapatite (HA). Therefore, purified insoluble bone collagen [α1(I)]2 α2 was degradated with cyanogen bromide. These CNBr peptides were purified further into five fractions, i.e., α2-CB2, α1-CB3, α1-CB6, α1-CB7 and α1-CB8 using CM-cellurose column chromatography and applied to HA column eluting with three different concentration of phosphate buffer (1/1000M to 1/10M : pH 6.8, step wise elution). The chromatographic evidences revealed the facts that each of the degradated peptide possessed characteristic interacting properties to HA, which was determined by eluting ratio with 1/1000M, 1/100M and 1/10M phosphate buffer. A peptide showed the weakest affinity to HA was α2-CB2 which was eluted out almost 94% of charged peptide by 1/1000M phosphate buffer. Close on 50 per cent of α1-CB3, however, had passed through with 1/1000M of the solution but still there was found more than 20 per cent of the peptide retained within HA column even after washing with 1/100M phosphate buffer. So far the eluting ratio of α1-CB6 and α1-CB7 was 5:27:68 (%) and 4:31:65 (%) espectively. These findings may possible to postulate that the CNBr peptides have adsorbing sites for HA which act as poly-functional mechanism depending on amino acid sequences. On the contrary to the facts mentioned above, the author emphasized the findings on bone collagen fragment which showed extreme affinity to the HA. This was α1-CB8 and 86 per cent of the peptide was solely released from HA by 1/10M phosphate buffer, which was, thereby, examined theoretically based on conformational investigations on collagen molecules. As the conclusion, the following sequences were tentatively predicated as adsorbing sites for HA : Arg (Lys)-X-Asp (Glu)-Asp (Glu, Thr, Ser) and Arg (Lis)-X-Y-Asp (Glu)-Asp (Glu, Thr, Ser).
Practice　： Dentistry
Keywords　：