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PMID: 6036530 Published · ppublish English Journal Article

High-resolution electron microscopic analysis of the amyloid fibril.

The Journal of cell biology ·Vol. 33 ·No. 3 ·1967-06-00 ·Pages 679-708

Shirahama T, Cohen AS

Abstract

The ultrastructural organization of the fibrous component of amyloid has been analyzed by means of high resolution electron microscopy of negatively stained isolated amyloid fibrils and of positively stained amyloid fibrils in thin tissue sections. It was found that a number of subunits could be resolved according to their dimensions. The following structural organization is proposed. The amyloid fibril, the fibrous component of amyloid as seen in electron microscopy of thin tissue sections, consists of a number of filaments aggregated side-by-side. These amyloid filaments are approximately 75-80 A in diameter and consist of five (or less likely six) subunits (amyloid protofibrils) which are arranged parallel to each other, longitudinal or slightly oblique to the long axis of the filament. The filament has often seemed to disperse into several longitudinal rows. The amyloid protofibril is about 25-35 A wide and appears to consist of two or three subunit strands helically arranged with a 35-50-A repeat (or, less likely, is composed of globular subunits aggregated end-to-end). These amyloid subprotofibrillar strands measure approximately 10-15 A in diameter.

MeSH Terms
Amyloidosis/pathology Humans Microscopy, Electron Microscopy, Polarization Spleen/pathology
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Shirahama T
Cohen A S
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1967-06-00
Pages
679-708
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2107207
Subset
IM
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