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PMID: 5123421 Published · ppublish English Journal Article

Creation of "amyloid" fibrils from Bence Jones proteins in vitro.

Science (New York, N.Y.) ·Vol. 174 ·No. 4010 ·1971-11-12 ·Pages 712-4

Glenner GG, Ein D, Eanes ED, Bladen HA, Terry W, Page DL

Abstract

"Amyloid" fibrils have been created from some human Bence Jones proteins by proteolytic digestion under physiologic conditions. These fibrils with an antiparallel, beta-pleated sheet conformation consist of only a portion of the variable region of the immunoglobulin light polypeptide chain and share the physical properties of amyloid fibrils. The relation between amyloidosis and immunoglobulins is thus more firmly established and a pathogenetic mechanism for amyloid fibril formation is suggested.

MeSH Terms
Amino Acid Sequence Amyloid/analysis,biosynthesis Bence Jones Protein/metabolism Humans Hydrogen-Ion Concentration In Vitro Techniques Microscopy, Electron Peptide Hydrolases Temperature X-Ray Diffraction
Chemicals
Amyloid Bence Jones Protein Peptide Hydrolases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Glenner G G
Ein D
Eanes E D
Bladen H A
Terry W
Page D L
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1971-11-12
Pages
712-4
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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