1968
DOI: 10.1177/16.10.633
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Amyloid. Vi. A Comparison of Two Morphologic Components of Human Amyloid Deposits

Abstract: Two morphologic components of human amyloid deposits, the periodic rod and the fibril, have been prepared free of cross-contamination. On tryptic digestion of guanidine-denatured material, peptide maps indicate these two components to have characteristic patterns with no detectable peptide fragments in common. Additional studies on ultrastructural morphology, physical characteristics and chemical composition reveal that the two components are cleanly distinct entities Method 2 C Fibrils Periodic Rods 634 GLENN… Show more

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Cited by 63 publications
(27 citation statements)
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“…These studies demonstrate that fibrils having the tinctorial, ultrastructural, and crystallographic properties (3)(4)(5) of amyloid fibrils can be created from some but not all Bence Jones proteins by peptic digestion at pH 3.5 and 370C. The results of peptide mapping, sequence analysis, and molecular weight determinations prove that these fibrils are derived solely from the variable region of the parent light chain.…”
mentioning
confidence: 73%
“…These studies demonstrate that fibrils having the tinctorial, ultrastructural, and crystallographic properties (3)(4)(5) of amyloid fibrils can be created from some but not all Bence Jones proteins by peptic digestion at pH 3.5 and 370C. The results of peptide mapping, sequence analysis, and molecular weight determinations prove that these fibrils are derived solely from the variable region of the parent light chain.…”
mentioning
confidence: 73%
“…Human amyloid deposits are rich in methionine and tryptophan [43]. Mouse Aβ, which lacks histidine and tyrosine, is less prone to aggregation than human Aβ [44].…”
Section: Toxicity and Amyloid Formationmentioning
confidence: 98%
“…The idea to test the EX material for crossreactivity with anti-amyloid was not utterly unfounded, but was a consequence of its amino acid 36 analysis (Ringvold 1973). Thus, with reference to the EX material it was stated in Ringvold's study (1973) that "-, a similar composition has been demonstrated in amyloid (Glenner et al 1968), in the microfibrillar component of elastic fibers (Ross & Bornstein 1966), in non-collagenous protein of basement membranes (Kefalides 1966), and others". In addition to this negative conclusion, the amino acid analysis suggested three other possibilities regarding the EX'S chemical nature.…”
Section: Examinations Evaluating the Ex Materialsmentioning
confidence: 99%