title: Factors influencing bonding of bromelain agglutinators and their Fab fragments.
abstract: The complex of bromelain agglutinators and their homologous Fab fragments is dissociated by gel chromatography under certain conditions. When albumin is present as a source of thiol groups, Fab fragments previously treated with N-ethylmaleimide (NEM) will dissociate from the agglutinators (fluid phase). If anti-Rh Fab fragments are bound to Rh-positive erythrocytes, the agglutinates are not dissociated by thiols (cellular phase). Prior to erythrocyte sensitization, the agglutinator site on Fab fragments can be blocked by thiol-disulfide exchange. Once the Fab fragments are coated on erythrocytes, the agglutinator site is more readily available than it was prior to sensitization, as evidenced by inhibition with 0.01 M NEM. The differences between the bonding characteristics of the fluid phase and the cellular phase and the influence of mercaptoalbumin on the agglutinator-Fab complex suggest that the agglutinators are not antibodies.
mesh_terms: D000888:Antibodies, Anti-Idiotypic / Q000276:immunology*; D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D001963:Bromelains / Q000276:immunology*; D002850:Chromatography, Gel; D004912:Erythrocytes / Q000166:cytology; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000276:immunology / Q000378:metabolism*; D011971:Receptors, Immunologic
chemical_list: D000888:Antibodies, Anti-Idiotypic; D007140:Immunoglobulin Fab Fragments; D011971:Receptors, Immunologic; D001963:Bromelains