Electron microscope investigations of the structure of collagen

The Structure of Human Skin Collagen as Studied With the Electron Microscope

“…2, the periods ranged from about 500 to 800 A, the maximum occurring between 620 and 660 A. This distribution is simil~r to that found by Nutting and Borasky (19) in cow skin fibrils; the range of variation is somewhat less than that found for the collagen of rat tail tendon by Schmitt, Hall, and Jakus (24). The average period in fibrils of adult skin does not appear to differ significantly from that of fibrils from infant skin.…”

“…Considerable attention has been devoted to the collagenous constituents. A periodically banded pattern was first demonstrated in electron micrographs of collagen fibrils in 1942 (11,24). The distance between repeating bands (axial period) agrees well with that previously demonstrated by Bear (2,3) and Kratky and Sekora (15) by x-ray diffraction methods.…”

“…1 thinner in young than in old individuals. The widths of fibrils of rat tail tendon range from almost as small as can be resolved by the electron microscope to 2,000 A and more (24). This variation probably reflects a real difference in the organization of the fibrils in different tissues rather than alterations due to the method of preparation.…”

The Behavior of Collagen Units as a Model in Morphogenesis

“…An exciting development was the revelation by electron microscopy that the reconstituted fibrils had the same precisely ordered morphology as did the native fibrils, namely the repeating axial period of about 640 A plus the detailed fine structure (1,21,38,42,51,52). The two aspects of the problem which have engaged the attention of most investigators in this area are the characterization of the molecule and elucidation of the mechanism of in vitro fibrogenesis with the hope of relating it to the in vivo physiological process.…”

Effects of lead on collagen synthesis and renal function in the rat

“…Dark bands are regions where charged groups bind the heavy metal stain and light bands are regions containing primarily uncharged residues (Bruns and Gross 1974). The axial period D was established variously as 64 nm (Bear 1942) or approximately 70 nm (Schmitt et al 1942); the variation is due to degree of fibril stretch and hydration. The currently accepted value for D seems to be 66.8 nm (Hodge and Schmitt 1960).…”