The rosettes formed by mouse peritoneal macrophages or DCH-5 cells and TNP-erythrocytes coated with anti-TNP antibodies of different isotypes were inhibited to various extent by monosaccharides. The most effective inhibitors were N-acetylglucosamine, glucosamine, mannose and N-acetylneuraminic acid in 1-5 mmol/L concentrations. Even more efficient were glycopeptides isolated from IgG molecules. The Fc receptors (FcRs) released from DCH-5 cells during cultivation and gradually separated by affinity chromatography on immobilized IgG reacted with aggregated IgG and inhibited the rosette formation. The FcRs eluted by monosaccharides influenced mainly the number of rosettes mediated by IgA and IgE while those eluted with a glycine-HCl buffer inhibited preferentially IgG rosettes. As shown by SDS-PAGE the heterogeneity of the fraction eluted with a mixture of monosaccharides revealed one main component with an effective molar mass of 50 kg/mol. The glycine-HCl eluate contained two major components of 55 and 38 kg/mol. The IgG-Sepharose 4B bound all the fractions but only the binding of the 50 kg/mol molecule could be inhibited by monosaccharides.

• MeSH
• Antigens, Differentiation metabolism   MeSH
• Glycopeptides metabolism   MeSH
• Immunoglobulin G chemistry   metabolism   MeSH
• Cells, Cultured MeSH
• Monosaccharides metabolism   MeSH
• Mice, Inbred A MeSH
• Mice MeSH
• Swine MeSH
• Receptors, Fc metabolism   MeSH
• Receptors, IgG MeSH
• Rosette Formation MeSH
• Animals MeSH
• Check Tag
• Mice MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Antigens, Differentiation MeSH
• Glycopeptides MeSH
• Immunoglobulin G MeSH
• Monosaccharides MeSH
• Receptors, Fc MeSH
• Receptors, IgG MeSH

A small part of polyclonal IgE (6%) was bound to protein A-Sepharose from the serum of M.P., containing a high concentration of IgE. No monoclonal IgE isolated from the serum of V.L. was bound to this sorbent. This binding of polyclonal IgE appears to be heterogeneous since a multiphasic pattern was observed with discontinuous pH gradient elution from protein A-Sepharose. Also, like IgE from the whole serum, monomeric IgE isolated from the serum of M.P. on Sepharose 6B showed this binding heterogeneity. It is suggested that IgE molecules with different affinities for protein A could belong to different isotypic or allotypic variants.

• MeSH
• Chromatography, Affinity MeSH
• Immunodiffusion MeSH
• Immunoglobulin E metabolism   MeSH
• Hydrogen-Ion Concentration MeSH
• Humans MeSH
• Staphylococcal Protein A metabolism   MeSH
• Binding Sites, Antibody MeSH
• Check Tag
• Humans MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Immunoglobulin E MeSH
• Staphylococcal Protein A MeSH

Addition of proteolysis inhibitors during the isolation procedure of rabbit arsanylated bovine IgG specific receptors decreased significantly the amount of low-molar-mass proteins in all receptor preparations. Rabbit ARS-BGG-specific receptor preparations isolated by immunoadsorption technique contain molecules which do not react with antigen and antibodies against immunoglobulins and have identical molar mass and chymotryptic peptide composition as those of isolated Fc receptors. It is suggested that during isolation of antigen-specific receptors from the surface of lymphoid cells, Fc receptors react with complexes composed of antigen and Ig+ receptors on the surface of immunoadsorbent and are isolated together with antigen-specific receptors.

• MeSH
• Phenylmethylsulfonyl Fluoride pharmacology   MeSH
• Immunoglobulin G immunology   MeSH
• Antigen-Antibody Complex immunology   MeSH
• Immunosorbent Techniques MeSH
• Rabbits MeSH
• Lymphocytes immunology   MeSH
• Receptors, Antigen immunology   isolation & purification   MeSH
• Receptors, Fc analysis   immunology   MeSH
• Cell Separation MeSH
• Sulfones pharmacology   MeSH
• Animals MeSH
• Check Tag
• Rabbits MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Phenylmethylsulfonyl Fluoride MeSH
• Immunoglobulin G MeSH
• Antigen-Antibody Complex MeSH
• Receptors, Antigen MeSH
• Receptors, Fc MeSH
• Sulfones MeSH

Proteins of pig serum and splenocytes which were isolated on immobilized guinea pig antibodies against human IgD were characterized by SDS-PAGE. In both cases the main isolated components possessed several properties nearly identical with those of human IgD: molar mass of the components and their chains, and susceptibility of the heavy chains, light chains, the chymotryptic peptide maps of the chains, and susceptibility of the heavy chains, the chymotryptic peptide maps of the chains, and susceptibility of the heavy chains in the native molecule to trypsin digestion. These IgD-like components not adsorbed on immobilized normal guinea-pig IgG. We suggest that the components of pig serum and splenocytes cross-reacting with highly specific antibodies against human IgD represent candidates for pig IgD. The percentage of the IgD-like molecules on the surface of pig splenocytes labeled with the antibody against human IgD was similar to the percentage of splenocytes bearing all immunoglobulins. Therefore, we suggest that IgD-like molecules were occurring on the surface of cells mostly together with molecules of another immunoglobulin class.

• MeSH
• Species Specificity MeSH
• Electrophoresis, Polyacrylamide Gel MeSH
• Immunoglobulin D immunology   MeSH
• Humans MeSH
• Lymphocytes immunology   MeSH
• Myeloma Proteins immunology   MeSH
• Swine immunology   MeSH
• Spleen cytology   immunology   MeSH
• Cross Reactions MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Immunoglobulin D MeSH
• Myeloma Proteins MeSH

Forty % of serum IgM and 47% of dimeric colostral IgA were bound to protein A-Sepharose. Fab mu and Fab alpha fragments showed a reactivity similar to that of the whole immunoglobulins. Complete elutions of IgM and IgA from the protein A-Sepharose were obtained in lower cocentrations of MgCl2 than the complete elution of IgG. However, IgM and IgA were completely eluted at higher concentrations of MgCl2 in the presence of IgG than in its absence.

• MeSH
• Chromatography, Affinity MeSH
• Magnesium pharmacology   MeSH
• Immunoglobulin A metabolism   MeSH
• Immunoglobulin M metabolism   MeSH
• Immunoglobulin alpha-Chains MeSH
• Immunoglobulin Fab Fragments * MeSH
• Immunoglobulin mu-Chains MeSH
• Swine MeSH
• Staphylococcal Protein A metabolism   MeSH
• Animals MeSH
• Check Tag
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Magnesium MeSH
• Immunoglobulin A MeSH
• Immunoglobulin M MeSH
• Immunoglobulin alpha-Chains MeSH
• Immunoglobulin Fab Fragments * MeSH
• Immunoglobulin mu-Chains MeSH
• Staphylococcal Protein A MeSH