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The structure and assembly of collagen fibrils *: II. An electron‐microscope study of cross‐linked collagen
Author(s) -
GRANT R. A.,
COX R. W.,
HORNE R. W.
Publication year - 1967
Publication title -
journal of the royal microscopical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.569
H-Index - 111
eISSN - 1365-2818
pISSN - 0368-3974
DOI - 10.1111/j.1365-2818.1967.tb04499.x
Subject(s) - fibril , electron microscope , collagen fibril , negative stain , staining , biophysics , macromolecule , type i collagen , chemistry , crystallography , scanning electron microscope , materials science , pathology , optics , biology , biochemistry , composite material , medicine , physics
SYNOPSIS An electron‐microscope study has been made of collagen fibrils before and after treatment with various cross‐linking reagents. In general it was found that cross‐linking resulted in an increase in the size of the light‐staining bands (as visualized by negative staining) and it was concluded that the light bands in native collagen correspond to regions where the tropocollagen macromolecules are bonded together. Treatment of the fibrous‐long‐spacing form of collagen resulted in the long period of 2300 Å being converted to a native‐type 640 Å periodicity.