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Science 12 November 1971:
Vol. 174. no. 4010, pp. 712 - 714
DOI: 10.1126/science.174.4010.712
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Articles

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

G. G. Glenner 1, D. Ein 1, E. D. Eanes 1, H. A. Bladen 1, W. Terry 1, and D. L. Page 1

1 National Institutes of Health, Bethesda, Maryland 20014

"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.


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Light chain-associated amyloid deposits comprised of a novel kappa  constant domain.
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The Cutaneous Amyloidoses: Pathogenesis and Therapy.
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Cryoglobulinemia and Amyloidosis Associated With Intestinal Lymphoma.
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Arch Intern Med 138, 1158-1160
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Renal Pathologic Findings Associated With Monoclonal Gammopathies.
A. Zlotnick and E. Rosenmann (1975)
Arch Intern Med 135, 40-45
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Repeated Immunization: Possible Adverse Effects: Reevaluation of Human Subjects at 25 Years.
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Electron Microscopy in the Diagnosis of Amyloidosis.
T. F. Goodman Jr., D. C. Abele, and C. S. West Jr. (1972)
Arch Dermatol 106, 393-397
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Y.-S. Kim, S. P. Cape, E. Chi, R. Raffen, P. Wilkins-Stevens, F. J. Stevens, M. C. Manning, T. W. Randolph, A. Solomon, and J. F. Carpenter (2001)
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Identification of a Heparin Binding Domain in the N-terminal Cleavage Site of Pro-islet Amyloid Polypeptide. IMPLICATIONS FOR ISLET AMYLOID FORMATION.
K. Park and C. B. Verchere (2001)
J. Biol. Chem. 276, 16611-16616
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