Xenopus laevis 19S immunoglobulin. Ultrastructure and J chain isolation.
Electron microscopy examination of the 19S immunoglobulin of Xenopus laevis revealed a hexameric structure with a central core. The molecules measured 360-430 A across the span of the arms and the average diameter of the central region was 140 A. A polypeptide, homologous to human J chain, was isolated by chromatography on DEAE-cellulose from the reduced and alkylated X. laevis hexameric macroglobulin. This polypeptide had a fast mobility in alkaline-urea gel electrophoresis, with distinct antigenicity, as compared to heavy and light chains. It shared common antigenic determinants with human J chain.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D000939:Epitopes; D007122:Immunoelectrophoresis; D007144:Immunoglobulin J-Chains / Q000302:isolation & purification*; D007075:Immunoglobulin M / Q000032:analysis*; D008854:Microscopy, Electron; D014981:Xenopus / Q000276:immunology*
D000939:Epitopes; D007144:Immunoglobulin J-Chains; D007075:Immunoglobulin M