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Abstract

The sequences of the 35 and 36 amino-terminal amino acids of two purified amyloid fibril proteins have been determined. Results indicate that these two proteins are derived from homogeneous immunoglobulin light chains of variable region subgroup VκI. The relation between amyloidosis and immunoglobulins is thus more firmly established.

References

APITZ, K, VIRCHOWS ARCH PATHOL 306: 631 (1940).
COHEN, A, PRELIMINARY CHEMICAL ANALYSIS OF PARTIALLY PURIFIED AMYLOID FIBRILS, LABORATORY INVESTIGATION 15: 66 (1966).
EANES, E.D., X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS, JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY 16: 673 (1968).
EDMAN, P, A PROTEIN SEQUENATOR, EUROPEAN JOURNAL OF BIOCHEMISTRY 1: 80 (1967).
FRANKLIN, E.C., MOLECULAR DEFECT IN A PROTEIN (CRA) FOUND IN GAMMA1 HEAVY CHAIN DISEASE, AND ITS GENETIC IMPLICATIONS, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 68: 187 (1971).
GLENNER, G, HUMAN AMYLOID PROTEIN - DIVERSITY AND UNIFORMITY, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 41: 1013 (1970).
GLENNER, G.G., AMYLOID PROTEIN - AMINO-TERMINAL VARIABLE FRAGMENT OF AN IMMUNOGLOBULIN LIGHT CHAIN, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 41: 1287 (1970).
GLENNER, G.G., AMYLOID .6. A COMPARISON OF 2 MORPHOLOGIC COMPONENTS OF HUMAN AMYLOID DEPOSITS, JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY 16: 633 (1968).
GLENNER, G.G., PHYSICAL AND CHEMICAL PROPERTIES OF AMYLOID FIBERS .2. ISOLATION OF A UNIQUE PROTEIN CONSTITUTING MAJOR COMPONENT FROM HUMAN SPLENIC AMYLOID FIBRIL CONCENTRATES, JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY 17: 769 (1969).
HARADA, M, JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY 19: 1 (1971).
HASS, G, Amyloid I Methods of isolating amyloid from other tissue elements, ARCHIVES OF PATHOLOGY 30: 240 (1940).
JANIGAN, D.T., EXPERIMENTAL AMYLOIDOSIS - ROLE OF ANTIGENICITY AND RAPID INDUCTION, AMERICAN JOURNAL OF PATHOLOGY 48: 1013 (1966).
MAGNUSLEVY, A, ZEITSCHRIFT FUR KLINISCHE MEDIZIN 116: 510 (1931).
MELLORS, R.C., ANALYTICAL PATHOLOGY .3. NEW OBSERVATIONS ON THE PATHOGENESIS OF GLOMERULONEPHRITIS, LIPID NEPHROSIS, PERIARTERITIS NODOSA, AND SECONDARY AMYLOIDOSIS IN MAN, AMERICAN JOURNAL OF PATHOLOGY 32: 455 (1956).
MILSTEIN, C, BIOCHEMICAL JOURNAL 101: 352 (1966).
MILSTEIN, C, LINKED GROUPS OF RESIDUES IN IMMUNOGLOBULIN K CHAINS, NATURE 216: 330 (1967).
Osserman, E. F., Cecil-Loeb Textbook of Medicine: 1113 (1967).
OSSERMAN, E. F., NEW ENGLAND JOURNAL OF MEDICINE 261: 1006 (1959).
OSSERMAN, E. F., SEMINARS IN HEMATOLOGY 1: 3 (1964).
PISANO, J.J., ANALYSIS OF AMINO ACID PHENYLTHIOHYDANTOINS BY GAS CHROMATOGRAPHY, JOURNAL OF BIOLOGICAL CHEMISTRY 244: 5597 (1969).
PRAS, M, CHARACTERIZATION OF SOLUBLE AMYLOID PREPARED IN WATER, JOURNAL OF CLINICAL INVESTIGATION 47: 924 (1968).
PRAS, M, PHYSICAL, CHEMICAL, AND ULTRASTRUCTURAL STUDIES OF WATER-SOLUBLE HUMAN AMYLOID FIBRILS - COMPARATIVE ANALYSES OF 9 AMYLOID PREPARATIONS, JOURNAL OF EXPERIMENTAL MEDICINE 130: 777 (1969).
SHIRAHAMA, T, HIGH-RESOLUTION ELECTRON MICROSCOPIC ANALYSIS OF AMYLOID FIBRIL, JOURNAL OF CELL BIOLOGY 33: 679 (1967).
VAZQUEZ, J. J., JOURNAL OF EXPERIMENTAL MEDICINE 104: 727 (1956).
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Science
Volume 172 | Issue 3988
11 June 1971

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Published in print: 11 June 1971

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G. G. Glenner
National Institutes of Health, Bethiesda. Maryland 20014
W. Terry
National Institutes of Health, Bethiesda. Maryland 20014
M. Harada
National Institutes of Health, Bethiesda. Maryland 20014
C. Isersky
National Institutes of Health, Bethiesda. Maryland 20014
D. Page
National Institutes of Health, Bethiesda. Maryland 20014

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  1. Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro, Science, 174, 4010, (712-714), (1971)./doi/10.1126/science.174.4010.712
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