Immunoglobulin D myeloma and amyloidosis: immunochemical and structural studies of Bence Jones and amyloid fibrillar proteins.
Blood. 1975 Nov; 46(5):713-22.Blood

Abstract

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.

Links

Publisher Full Text
linkinghub.elsevier.com
ashpublications.org

Authors

White GC
No affiliation info available
Jacobson RJ
No affiliation info available
Binder RA
No affiliation info available
Linke RP
No affiliation info available
Glenner GG
No affiliation info available

MeSH

AgedAmyloidAmyloidosisBence Jones ProteinCervical VertebraeDiaphragmFractures, SpontaneousHumansImmunoglobulin delta-ChainsImmunoglobulin lambda-ChainsIntestinal MucosaKidneyLungMaleMultiple MyelomaMuscle, SmoothPeptide Chain Termination, Translational

Pub Type(s)

Case Reports
Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

809071