CRYSTALLINITY AND CRYSTALLOGRAPHIC FIBER PERIOD OF COLLAGEN FIBER WITH AGING
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概要
- 論文の詳細を見る
Scott et. al. obtained the following interesting results about aging of rat tail tendon. They stained a proteoglycan in rat tail tendon by caproic acid and observed it using an electron microscope. The proteoglycan could be seen as like a fiber which is coiled around collagen fibril perpendicular to the axis. The interval of the proteoglycan increased with aging, and the content of the proteoglycan decreased with aging. A question could be raised whether the crystallographic fiber period of collagen fiber itself changes with aging. We may expect that the amino acid sequence of tropocollagen could not be changed with aging because its gene expression would not change with aging and the period does not change. However, this is not self-evident. This must be confirmed experimentally. This question could be clarified by the x-ray small angle scattering method (XSAS). We define here the crystallographic fiber period as a spacing which can be determined by x-ray small angle scattering of the first order reflection. It is usually about 64nm. This paper will deal the fiber period, the sharpness of the diffraction spots and the diffuseness of the amorphous halo which attributes to proteoglycan.. And we obtained the following results. The X-ray Small angle Scattering method disclosed that the crystallographic fiber period of gerbil tai tendon collagen did not change with aging. Two kinds of scattering profiles were recognized; crystalline diffraction spots and the amorphous diffuse scattering halo. The crystalline diffraction spots were broad in a younger tendon. However, they became shaper with aging. The amorphous diffuse halo that is marked in young tendon diminishes with aging. these results indicate that 1; the collagen fiber of a young tendon contains many crystal defects, 2; the content of proteoglycan in a younger tendon is higher than that in an older tendon . The X-ray diffraction profiles become clear with aging. Similar phenomena were also recognized in domestic fowl, therefore they should be common nature of collagen fiber in species.
- 日本結合組織学会の論文
著者
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Tanaka Ki-ichiro
Dep. Of Oral Biochemistry School Of Dentistry Nagasaki Univ.
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Ono Toshio
Dep. of Oral Biochemistry, School of Dentistry, Nagasaki Univ.
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Ono Toshio
Dep. Of Oral Biochemistry School Of Dentistry Nagasaki Univ.