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天然胶原蛋白的超微结构。

Ultrastructure of native collagen.

作者信息

Bocciarelli D S

出版信息

Ann Ist Super Sanita. 1974;10(3-4):191-202.

PMID:4470988
Abstract

Native collagen fibrils, mechanically detached either from leg tendon of rabbits or from tail tendon or aortic adventitia of adult rats were observed at the electron microscope by various technical methods. The density patterns recorded along and across integer fibrils, laid down on ultrathin C films, show that the density ratio of the light to the dense bands is much higher than that expected from the generally accepted quarter-stagger arrangement of collagen unities. Swollen fibrils show long filaments, about 50 A thick, reasonably identified with their building unities. The characteristic collagen banding of about 640 A periodicity, never exhibited by single filaments, is already present in groups of very few filaments (order of two or three). Partially disrupted fibrils suggest that the building filaments may be assembled in a monolayer, having the form of a long ribbon, spirally wound around the longitudinal axis of the integer fibril.

摘要

通过各种技术方法,在电子显微镜下观察了从兔腿肌腱、成年大鼠尾腱或主动脉外膜机械分离出的天然胶原纤维。沿着和横跨放置在超薄C膜上的完整纤维记录的密度模式表明,亮带与暗带的密度比远高于从普遍接受的胶原单体四分之一交错排列所预期的密度比。肿胀的纤维显示出约50埃厚的长丝,合理地认为它们与构成单位一致。约640埃周期性的特征性胶原条纹,单根丝从未显示过,在非常少的丝束(两到三根的数量级)中就已经存在。部分破坏的纤维表明,构成丝可能以单层形式组装,呈长带状,围绕完整纤维的纵轴螺旋缠绕。

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