The Tubular Structure of Collagen Fibril

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Collagen Fibril Formation

Soluble rat tail tendon collagen with intact nonhelical ends and largely free of aggregates was used to study fibril formation in vitro. The process was initiated by raising the pH and warming a cold solution of collagen. Fibril formation was monitored by turbidity and the product was examined by electron microscopy. Optimal conditions that will form fibrils similar to those observed in vivo ar...

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Collagen structure: evidence for a helical organization of the collagen fibril.

The collagen fibrils of human or guinea pig dermis when exposed to the denaturing agents, urea or guanidine-HC1, dissociated into smaller, disparate subunits, probably aggregates of microfibrils. The process of dissociation demonstrates that the fibrils are assembled helically. Initially, diagonal clefts appear on the surface of the fibril. These clefts are surface manifestations of a spirally ...

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Collagen fibril formation.

Collagen is most abundant in animal tissues as very long fibrils with a characteristic axial periodic structure. The fibrils provide the major biomechanical scaffold for cell attachment and anchorage of macromolecules, allowing the shape and form of tissues to be defined and maintained. How the fibrils are formed from their monomeric precursors is the primary concern of this review. Collagen fi...

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Electron microscopy shows periodic structure in collagen fibril cross sections.

X-ray diffraction was used to monitor the effects of electron microscope fixation, staining, and embedding procedures on the preservation of the three-dimensional crystalline order in collagen fibrils of rat tail tendon. A procedure is described in which the characteristic 3.8-nm lateral spacing is preserved, with increased contrast, in the diffraction pattern of the embedded fiber. This spacin...

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ژورنال

عنوان ژورنال: Bulletin of the Chemical Society of Japan

سال: 1962

ISSN: 0009-2673,1348-0634

DOI: 10.1246/bcsj.35.769