Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro

Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro

"Amyloid" fibrils have been created from some human Bence Jones proteins by proteolytic digestion under physiologic conditions. These fibrils with an antiparallel, β-pleated sheet conformation consist of only a portion of the variable region of the immunoglobulin light polypeptide chain an...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1971-11, Vol.174 (4010), p.712-714
Hauptverfasser: Glenner, G. G., Ein, D., Eanes, E. D., Bladen, H. A., Terry, W., Page, D. L.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Amino acids
Amyloid - analysis
Amyloid - biosynthesis
Amyloidosis
Amyloids
Bence Jones Protein - metabolism
Cell lines
Humans
Hydrogen-Ion Concentration
Immunoglobulins
In Vitro Techniques
Microscopy, Electron
Muscle fibers
Peptide Hydrolases
Ploidies
Solar fibrils
Stem cells
Temperature
Tumor cell line
X-Ray Diffraction
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Zusammenfassung:"Amyloid" fibrils have been created from some human Bence Jones proteins by proteolytic digestion under physiologic conditions. These fibrils with an antiparallel, β-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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.174.4010.712