A comparison of secretory component - immunoglobulin interactions amongst different species.
1) SC from many species may be isolated by affinity chromatography to human IgA-Sepharose. 2) In some species SC may exist in two molecular forms. 3) The SC-binding sites on polymeric IgA and IgM are not identical. 4) In some species SC binds to IgM with higher affinity than to polymeric IgA while in other species SC binds best to polymeric IgA. This difference may influence the relative concentrations of these two immunoglobulin classes in the secretions of different species. 5) The SC-binding site is present on high molecular weight immunoglobulin in species as primitive as the nurse shark.
D000818:Animals; D001665:Binding Sites; D006801:Humans; D007070:Immunoglobulin A / Q000378:metabolism*; D007128:Immunoglobulin Fragments / Q000378:metabolism*; D007075:Immunoglobulin M / Q000378:metabolism*; D007526:Isoelectric Point; D010802:Phylogeny; D011485:Protein Binding; D012635:Secretory Component / Q000302:isolation & purification / Q000378:metabolism*; D013045:Species Specificity
D007070:Immunoglobulin A; D007128:Immunoglobulin Fragments; D007075:Immunoglobulin M; D012635:Secretory Component