Immunoglobulin D myeloma and amyloidosis: immunochemical and structural studies of Bence Jones and amyloid fibrillar proteins.
Urinary Bence Jones protein and amyloid fibril protein isolated from the subcutaneous tissue of a patient with IgD myeloma and associated amyloidosis were subjected to physicochemical and immunochemical identification. Peptide maps and amino-terminal tetrapeptide composition obtained from the two proteins were comparable. Immunochemical cross-reactivity between the two proteins, with other lambda-type amyloid and Bence Jones proteins, and with a serum component was demonstrated. The results suggest that the source of the amyloid fibril protein is an intact circulating light polypeptide chain as well as smaller amino-terminal fragments.
D000368:Aged; D000682:Amyloid / Q000032:analysis*; D000686:Amyloidosis / Q000209:etiology*; D001536:Bence Jones Protein / Q000652:urine*; D002574:Cervical Vertebrae / Q000293:injuries; D003964:Diaphragm / Q000473:pathology; D005598:Fractures, Spontaneous; D006801:Humans; D007138:Immunoglobulin delta-Chains; D007146:Immunoglobulin lambda-Chains; D007413:Intestinal Mucosa / Q000473:pathology; D007668:Kidney / Q000473:pathology; D008168:Lung / Q000473:pathology; D008297:Male; D009101:Multiple Myeloma / Q000150:complications*; D009130:Muscle, Smooth / Q000473:pathology; D010443:Peptide Chain Termination, Translational
D000682:Amyloid; D007138:Immunoglobulin delta-Chains; D007146:Immunoglobulin lambda-Chains; D001536:Bence Jones Protein