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6 results on '"Ein D"'

4. Amino acid sequence of an amyloid fibril protein of unknown origin.

Author

Ein D, Kimura S, Terry WD, Magnotta J, and Glenner GG

Subjects
Amino Acids analysis, Chromatography, Thin Layer, Chymotrypsin, Dansyl Compounds, Humans, Hydrazines, Peptides analysis, Peptides isolation & purification, Trypsin, Amino Acid Sequence, Amyloid analysis
Published
1972

5. The immunoglobulin origin of amyloid.

Author

Glenner GG, Ein D, and Terry WD

Subjects
Amino Acid Sequence, Amyloidosis drug therapy, Amyloidosis metabolism, Antigen-Antibody Complex, Aspartic Acid metabolism, Bence Jones Protein, Bone Neoplasms immunology, Cyclophosphamide therapeutic use, Fluorescent Antibody Technique, Humans, Melphalan therapeutic use, Molecular Weight, Multiple Myeloma immunology, Myeloma Proteins, Peptides metabolism, Plasma Cells, Polysaccharides metabolism, Ultracentrifugation, Amyloid analysis, Amyloidosis immunology, Immunoglobulins
Published
1972
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6. Creation of "amyloid" fibrils from Bence Jones proteins in vitro.

Author

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

Subjects
Amino Acid Sequence, Amyloid analysis, Humans, Hydrogen-Ion Concentration, In Vitro Techniques, Microscopy, Electron, Peptide Hydrolases, Temperature, X-Ray Diffraction, Amyloid biosynthesis, Bence Jones Protein metabolism
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.

Published
1971
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