Structural studies of the Xenopus 19S immunoglobulin and 7S immunoglobulin and two immunoglobulin-like proteins.
Xenopus laevis 19S and 7S immunoglobulins (Ig) were extensively reduced and alkylated, their H and L chains spearated and their molecular weights determined. Two kinds of L chains of molecular weight 25,000 and 27,000 were revealed by SDS-polyacrylamide gel electrophoresis. In addition two Ig-like proteins consisting of heavy chains only, of 19S H-type and with similar molecular weight, were detected in Xenopus serum ans isolated. These proteins share common antigenic determinants with Xenopus 19S Ig heavy chains and are devoid of light chain determinants.
D000478:Alkylation; D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D005260:Female; D006801:Humans; D007122:Immunoelectrophoresis; D007128:Immunoglobulin Fragments / Q000302:isolation & purification*; D007143:Immunoglobulin Heavy Chains / Q000302:isolation & purification; D007146:Immunoglobulin lambda-Chains / Q000302:isolation & purification; D008297:Male; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011817:Rabbits / Q000276:immunology; D014981:Xenopus / Q000276:immunology*
D000939:Epitopes; D007128:Immunoglobulin Fragments; D007143:Immunoglobulin Heavy Chains; D007146:Immunoglobulin lambda-Chains