アブストラクト（7巻3号：神奈川歯学）

神奈川歯学

Japanese

Title　： 結合組織の生化学的研究 - 特に牛アキレス腱の遊離アミノ酸とペプチド構成アミノ酸について -
Subtitle　：
Authors　： 高木亨, 日比野陽三, 斉藤滋
Authors（kana）　：
Organization　： 神奈川歯科大学口腔生化学教室
Journal　： 神奈川歯学
Volume　： 7
Number　： 3
Page　： 178-188
Year/Month　： 1972 / 9
Article　： 報告
Publisher　： 神奈川歯科大学学会
Abstract　： 「抄録」 結合組織に含まれるコラーゲンは生物化学的及び分子生物学的立場からその結合組織構成物質の分子構造及び生合成に関し広く研究されているが, これらの生理的崩壊機序及び組織特異性に関する研究は極めて少なく, 我々はそれらを知る先ず第1の手段として0.2M Na2HPO4より抽出された牛アキレス腱の透析性蛋白分屑について歯根膜と比較し検討した. アキレス腱に於ける遊離アミノ酸は乾燥単位重量に対し約1/100μM/gのオーダーで存在し, Tyrosine, Phenylalanine及びhistidineが主要遊離アミノ酸として64%をしめ, 又Hydroxyproline及びHydroxylysine比は分子構成比の近似値として存在した. ペプチド構成アミノ酸は約1/10μM/g(dry weight)のオーダーで存在し, Asparatic Acid, Glutamic Acid及びGlycineが全体の35%をしめる主要構成アミノ酸で存在した. これら主要構成アミノ酸は遊離での存在量は少なく約40倍以上がBound Formとして存在した. 更に乾燥単位重量当たり存在する全ペプチド構成アミノ酸と全遊離アミノ酸の存在モル比は4:1となり低分子ペプチドから遊離アミノ酸への崩壊が極めてInactiveであることが推定された. 更にHydroxy Proline及びHydrxylysineの結合型と遊離型の存在比がそれぞれ5:1, 2:1とCollagenの生理的崩壊を示す正常値を得た. これら牛アキレス腱の分布を歯根膜と比較検討すると, 遊離アミノ酸で歯根膜は腱より10～100倍多く存在しHydoxyprolineは腱の2倍存在する組織特異性を示した. 又歯根膜のペプチド構成アミノ酸は1/10～1μM/g(dry weight)存在し, Asparatic Acid, Lysine及びThreonineが全体の55%を占める主要構成アミノ酸であり, Asparatic Acid及びGlutamic Acidはアキレス腱でも主要構成アミノ酸として存在し共通の蛋白成分の存在を認めた. 更にHydroxyproline及びHydroxylysineの構成比は歯根で1:1であるのに対しアキレス腱は一般的に知られるコラーゲンの構成比に類似し両組織でのコラーゲンの生理的崩壊機序の相異性を示した.
Practice　： 歯科学
Keywords　：

English

Title　： Biochemical Investigation of Connective Tissue - Free Amino Acids and Peptide Amino Acids Composition of Bovine Achilles Tendon
Subtitle　：
Authors　： Tohru Takagi, Yozo Hibino, Shigeru Saito
Authors（kana）　：
Organization　： Dept.of Oral Biochemistry, Kanagawa Dental College
Journal　： Kanagawa Shigaku
Volume　： 7
Number　： 3
Page　： 178-188
Year/Month　： 1972 / 9
Article　： Report
Publisher　： Kanagawa Odontological Society
Abstract　： Recently, it has been well studied on the fibrous main component of connective tissues -collagen- concerning its molecular structure and biosynthetic pass way in term of physicochemical and medical point of views. However, in the most of type of connective tissue disease, especially, concerning oral tissue destruction of variovs intercellular elements is a prominent feature of the disease, a mechanisms of physiological break down of collagen in the tissues are still remined uncertain. In order to understand the mechanism and a specificity of the tissue, as the first step of expriment, bovine achilles tendon were extracted with 0.2 M Na2 HPO4 and examined a amino acids composition of dialyzable fraction-free and peptide amino acids in comparison of the same fraction of periodontal membrane. For free amino acids, tyrosine, phenylalanine and histidine were the major component which were accounted for 64 per cent of total free amino acids and others were contained approximately 1/100 μM per gram of dry weight tissue. Asparatic acid, gultamic acid and glycine were 35 per cent of total peptide amino acids, which were the major amino acids composing peptides. These were found about 40 times of the free amino acids, and the moler ratio of total peptide amino acids and free amino acids were 4:1. This suggests that catabolic change of peptide to free amino acids were inactive. The ratio of free amino acid / peptide bound amino acid and hydroxyproline / hydroxylysine were 5:1 and 2:1 respectively, with which, one can asume, interceller protein component in physiolgicol state of achilles tendon were degradated. In comparsion of these amino acids to the periodontal menbrane, there were ovserved a clear tissue specificity between these, i.e., as for as a total μM of free amino acids existing in unite weight of dry tissue, periodontal membrane contained 10-100 times more than that of tendon, however hydroxyproline existing in periodontal menbrane were about twice much more than that of tendon. For peptide amino acids, major component were asparatic acid, lysine and threonine which were occupied 55 per cent of total peptide amino acids. And others were distributed in a range of 1/10 to 1 μM order. The two hydroxylated imino acid specific for collagen were found in the some amount of moles, which strongly indicate the fact that the differences of catabolic mechanisms were physiologically proceeding in those tissues.
Practice　： Dentistry
Keywords　：