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Quantitative electron microscope observations of the collagen fibrils in rat‐tail tendon
Author(s) -
Parry D. A. D.,
Craig A. S.
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360160506
Subject(s) - fibril , collagen fibril , electron microscope , tendon , chemistry , anatomy , biophysics , collagen fibres , transmission electron microscopy , crystallography , materials science , optics , nanotechnology , biochemistry , biology , physics
An electron microscope study of collagen fibrils from fixed tail tendons of rats has revealed that from some time shortly after birth until maturity, the fibril diameters have a bimodal distribution. The “two” types of fibril are indistinguishable in both transverse and longitudinal section. Unfixed specimens of eight‐week‐old‐tail tendon showed a similar bimodal distribution of diameters though the positions of the peak values compared to fixed specimens of an eight‐week‐old‐tail tendon were shifted upwards by about 30%. It has also been shown quantitatively that the polar collagen fibrils are directed randomly “up” and “down” with respect to their neighbors. Whilst it has been suggested by others that anastomosis is a feature of collagen structure, the results presented here do not support this hypothesis. Fibrillar units ∼ 140 Å in diameter have been observed and the possibilities that these are elastic fibers or the breakdown products of collagen fibrils have been considered.