Demonstration and partial characterization of an atypical protein in the urine of a patient with primary amyloidosis.
A paraprotein has been isolated from the urine of a patient with primary amyloidosis. Immunologically it was classified as a free lambda light chain. The molecular weight was 22500 daltons. N-terminal amino acid analysis demonstrated homology with lambda IV variable subgroup in 19 of the first 20 amino acids. Extensive homology with lambda IV chains was demonstrated also in the hypervariable region of the light chain. An antiserum produced against the paraprotein was rendered idiotype-specific by absorption with pooled human light chains. This antiserum stained tissue specimen from the rectum and liver of the patient by the indirect immunofluorescence technique. This strongly indicates that the free lambda light chains that can be isolated from the urine are also deposited in the tissues as amyloid substance.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000686:Amyloidosis / Q000652:urine*; D004587:Electrophoresis, Agar Gel; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods; D005455:Fluorescent Antibody Technique; D006801:Humans; D007147:Immunoglobulin Light Chains / Q000302:isolation & purification; D007146:Immunoglobulin lambda-Chains / Q000302:isolation & purification; D008297:Male; D008875:Middle Aged; D008970:Molecular Weight; D010266:Paraproteins / Q000276:immunology / Q000302:isolation & purification / Q000652:urine*
D000596:Amino Acids; D007147:Immunoglobulin Light Chains; D007146:Immunoglobulin lambda-Chains; D010266:Paraproteins