Abstract
SINCE the original observations of Cohen and Calkins1, recent electron microscopic investigations have clearly confirmed the fact that amyloid of all types so far examined possess a fibrous ultrastructure. However, some differences in measurements of the dimensions of amyloid fibrils in tissue sections (50–300 Å) have been reported and no clear delineation of sub-unit structure has been available2–8. This communication deals with the fact that after negative staining the ultrastructure of the amyloid fibril can be resolved to filaments, laterally aggregated in varying numbers, in a manner that would explain the aforementioned differences.
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References
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SHIRAHAMA, T., COHEN, A. Structure of Amyloid Fibrils after Negative Staining and High-resolution Electron Microscopy. Nature 206, 737–738 (1965). https://doi.org/10.1038/206737a0
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DOI: https://doi.org/10.1038/206737a0
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