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Chemical Evidence for -Type Amyloid Fibril Proteins

From the Section on Molecular Pathology, National Institute of Arthritis and Metabolic Diseases and National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014

Abstract

A group of proteins comprising the major component of human amyloid fibrils have been shown to have antigenic determinants in common with the amino terminal segment of immunoglobulin light polypeptide chains (1). On the basis of these immunochemical studies amyloid proteins of immunoglobulin origin have been designated as either of - or -type. Automatic amino acid sequence analysis has demonstrated that the -type amyloid fibril proteins are homologous with the amino terminal protion of a -Bence Jones (BJ)³ protein (2, 3).

Amyloid fibril proteins isolated from four patients have been fractionated by gel filtration to purity as defined by the presence of a single band on sodium dodecyl sulfate polyacrylamide disc gel electrophoresis (4). Immunochemical analysis of these four preparations showed reactions consistent with the presence of -light chains (1) and chemical analysis indicated that the polypeptide chains in these preparations had unreactive amino terminal residues (4).

Footnotes

³ Abbreviations used in this paper: BJ, Bence-Jones; Glp-Ala, pyrrolidonylalanine; DNFB, dinitrofluorobenzene.

¹ Visiting Fellow in Molecular Pathology, Nagoya City University School of Medicine, Department of Biochemistry, Mizuhoku, Nagoya, Japan.

² Please address all communications to Dr. George G. Glenner, Chief, Section on Molecular Pathology, Building 10, Room 3N-112, Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014.