Nonprecipitating pig anti‐dinitrophenyl antibody: Factors influencing the conversion into precipitating antibody

A high affinity nonprecipitating anti‐2,4‐dinitrophenyl (DNP) IgG antibody constitutes a major fraction of circulating anti‐DNP antibodies at the decline of the anti‐ DNP antibody response in pigs. The purified nonprecipitating antibody forms exclusively soluble complexes with DNP‐PSA (pig serum albumin) or DNP‐PGG (pig IgG). The binding sites are accessible to large ligands; one antibody molecule can combine with two molecules of DNP‐PSA simultaneoulsy.

[1]  M. Saber,et al.  Non-antibody components in porcine anti-DNP antibody preparations obtained by affinity chromatography. , 1979, Molecular immunology.

[2]  J. Novotný,et al.  Distance between two binding sites of the molecule: a neutron small-angle scattering study of pig anti-Dnp antibody complexed with mono-Dnp-dextran. , 1978, FEBS letters.

[3]  E. Dudich,et al.  Fluorescence polarization analysis of various immunoglobulins Dependence of rotational relaxation time on protein concentration and on ability to precipitate with antigen , 1978, FEBS letters.

[4]  J. Novotný,et al.  Neutron small‐angle scattering study on two different precipitin types of pig Anti‐Dnp antibodies , 1977, FEBS letters.

[5]  R. Falk,et al.  Conversion of incomplete antibodies to direct agglutinins by mild reduction: evidence for segmental flexibility within the Fc fragment of immunoglobulin G. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[6]  G. Füst,et al.  Complement consumption by immune complexes containing various pig anti-DNP antibodies and DNP-serum albumin. , 1977, Immunochemistry.

[7]  F. Franek,et al.  Different types of precipitating antibodies in early and late porcine anti-dinitrophenyl sera. , 1974, Immunochemistry.

[8]  G. Edelman Antibody structure and molecular immunology. , 1973, Science.

[9]  J. Harrington,et al.  Polymer-induced precipitation of antigen-antibody complexes: "precipiplex" reactions. , 1971, Immunochemistry.

[10]  F. Franek Affinity labeling by m-nitrobenzenediazonium fluoroborate of porcine ANTI-dinitrophenyl antibodies. Position of labeled tyrosine in the lambda-chains. , 1971, European journal of biochemistry.

[11]  K. Hellsing Immune reactions in polysaccharide media. The effect of hyaluronate, chondroitin sulphate and chondroitin sulphate-protein complex on the precipitin reaction. , 1969, The Biochemical journal.

[12]  F. Karush,et al.  Equine anti-hapten antibody-V the non-precipitability of bivalent antibody , 1967 .

[13]  A. Nisonoff,et al.  Heterogeneity in the complementation of polypeptide subunits of a purified antibody isolated from an individual rabbit. , 1966, Journal of immunology.

[14]  H. Eisen,et al.  THE PREPARATION AND SOME PROPERTIES OF PURIFIED ANTIBODY SPECIFIC FOR THE 2,4-DINITROPHENYL GROUP , 1960, The Journal of experimental medicine.

[15]  W. Weigle,et al.  The effect of complements on soluble antigen-antibody complexes. , 1957, Journal of immunology.

[16]  S. Belman,et al.  The Reaction of 2,4-Dinitrobenzenesulfonic Acid with Free Amino Groups of Proteins , 1953 .

[17]  J. Ovádi,et al.  Macromolecular interactions in enzyme regulation. , 1976, Advances in enzyme regulation.

[18]  F. Franek,et al.  The antibody response of pigs to dinitrophenylated bovine IgG administered with a novel type of adjuvant , 1971, European journal of immunology.

[19]  F. Franek,et al.  On proteins. CX. Isolation and characterization of λ- and π-chains representing structural types of pig γG-globulin light chains , 1967 .

[20]  T. Laurent,et al.  The Influence of Dextran on the Precipitin Reaction. , 1964 .