Electron microscope evidence for an 80 A unit in collagen fibrils.
Connective tissues are composite structures containing collagen, elastin, glycosaminoglycans, minerals, water and other minor components. In all cases the collagen exists predominantly in fibrillar form. The size distribution of the fibrils does, however, vary markedly with both age and the mechanical requirements of the tissue. Little is known about the mechanism of fibril formation in vivo, although some information is now available form in vitro polymerisation studies. We have now collected new and extensive electron microscope data on the size of collagen fibrils from tendon, skin, cornea and other tissues from both fetal and immature animals. The results reported here show that the diameters of the collagen fibrils thus measured lie close to a multiple of 80 A, a result which may be simply and readily interpreted in terms of the collagen microfibril and its mode of packing.
D000818:Animals; D003094:Collagen; D003238:Connective Tissue / Q000648:ultrastructure*; D003315:Cornea / Q000648:ultrastructure; D006801:Humans; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009412:Nerve Fibers / Q000648:ultrastructure; D011485:Protein Binding; D012867:Skin / Q000648:ultrastructure; D013710:Tendons / Q000648:ultrastructure
D046911:Macromolecular Substances; D003094:Collagen