Phylogenetic origins of immune recognition: naturally occurring DNP-binding molecules in chordate sera and hemolymph.
A method is described which allows the isolation of small quantities of DNP-binding antibodies of both high- and low-molecular-weight classes. The only detectable DNP-binding protein in the serum of placoderm-derived vertebrates was immunoglobulin in nature, and of the order of less than or equal to 1% total serum immunoglobulin. Proteins in the serum of the urochordate Pyura stolonifera, which bind to both DNP and erythrocyte antigens, showed charge heterogeneity and an apparent subunit molecular weight of approximately 65,000 to 70,000 daltons.
D000818:Animals; D001666:Binding Sites, Antibody; D002816:Chordata, Nonvertebrate; D004136:Dinitrobenzenes / Q000276:immunology*; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000276:immunology; D006458:Hemolymph / Q000276:immunology*; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D051379:Mice; D008808:Mice, Inbred CBA; D009578:Nitrobenzenes / Q000276:immunology*; D010802:Phylogeny; D011485:Protein Binding; D011817:Rabbits; D012756:Sheep
D004136:Dinitrobenzenes; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D009578:Nitrobenzenes