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Research Article Free access | 10.1172/JCI107295
Immunology Branch, National Cancer Institute and Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland 20014
Institute of Cancer Research and Department of Medicine, Columbia University College of Physicians and Surgeons, New York 10032
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Immunology Branch, National Cancer Institute and Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland 20014
Institute of Cancer Research and Department of Medicine, Columbia University College of Physicians and Surgeons, New York 10032
Find articles by Page, D. in: JCI | PubMed | Google Scholar
Immunology Branch, National Cancer Institute and Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland 20014
Institute of Cancer Research and Department of Medicine, Columbia University College of Physicians and Surgeons, New York 10032
Find articles by Kimura, S. in: JCI | PubMed | Google Scholar
Immunology Branch, National Cancer Institute and Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland 20014
Institute of Cancer Research and Department of Medicine, Columbia University College of Physicians and Surgeons, New York 10032
Find articles by Isobe, T. in: JCI | PubMed | Google Scholar
Immunology Branch, National Cancer Institute and Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland 20014
Institute of Cancer Research and Department of Medicine, Columbia University College of Physicians and Surgeons, New York 10032
Find articles by Osserman, E. in: JCI | PubMed | Google Scholar
Immunology Branch, National Cancer Institute and Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland 20014
Institute of Cancer Research and Department of Medicine, Columbia University College of Physicians and Surgeons, New York 10032
Find articles by Glenner, G. in: JCI | PubMed | Google Scholar
Published May 1, 1973 - More info
The partial amino acid sequence of the amyloid fibril protein isolated from the small intestine of a patient with plasma cell dyscrasia and associated amyloidosis has been determined and compared with the sequence of the κ-type Bence Jones protein isolated from the urine of the same patient. Identical sequences were observed for the 27 amino-terminal residues that could be compared. The C-terminal tryptic peptide of the amyloid protein was identical with that of the Bence Jones protein. Apparent molecular weights and amino acid compositions of the Bence Jones and amyloid proteins were similar. It appears, therefore, that the predominant protein present in the amyloid deposits in this patient was an intact κ-type light polypeptide chain that was identical with the urinary Bence Jones protein.
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