Murine Gc globulin binds to a synthetic sequential polypeptide that is a murine B lymphocyte mitogen.
A non-immunoglobulin component in mouse serum was found to compete with antibody for the binding of a polyanionic antigen, poly (Tyr-Glu-Ala-Gly). The percent of the polymer (44 ng/ml) bound at physiological pH by the serum component in normal mouse serum was low (18%), but was much higher at pH 6.0 (85%). As a result, the binding of the polyanionic peptide antigen by antibody in immune serum was considerably lower at pH 6.0 than it was at physiological pH. These results should be taken into account when dealing with similar antigens that have been frequently studied in immunology, such as poly (Glu60 Ala40) and poly (Glu60 Ala30 Tyr10). The non-immunoglobulin serum component has been identified as Gc globulin, a vitamin D-binding protein that has been shown to be present on the surface of B lymphocytes. This binding might be responsible for the murine B cell mitogenicity of poly (Tyr-Glu-Ala-Gly) that has been previously reported.
D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology*; D002846:Chromatography, Affinity; D006863:Hydrogen-Ion Concentration; D007106:Immune Sera / Q000276:immunology; D051379:Mice; D008810:Mice, Inbred C57BL; D008934:Mitogens / Q000378:metabolism*; D010455:Peptides / Q000276:immunology / Q000378:metabolism*; D014809:Vitamin D-Binding Protein / Q000097:blood* / Q000302:isolation & purification
D007106:Immune Sera; D008934:Mitogens; D010455:Peptides; D014809:Vitamin D-Binding Protein; C051032:poly(tyrosyl-glutamyl-alanyl-glycyl)