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A NISONOFF

Publications and source records attributed to A NISONOFF.

At least 19 recordsLinked to original sources

LATTICE FORMATION IN COMPLEMENT FIXATION: STUDIES WITH UNIVALENT RABBIT ANTIBODY.

Hybrid univalent 6.5S antibody molecules, formed by recombination of half-molecules of rabbit antibody to ovalbumin with those of normal rabbit gamma(G)-globulin, fail to fix complement in reactions with homologous antigen. Such hybrid molecules, however, block complement fixation by intact antibody to ovalbumin. Molecules of antibody reconstituted in the absence of other protein retain the capacity to fix complement. The data suggest that small complexes containing excess univalent antibody do not fix complement and that lattice formation is required for fixation.

Animals↗

HYBRIDIZATION OF HALF MOLECULES OF RABBIT GAMMA GLOBULIN.

Specifically purified rabbit antiovalbumin and normal gamma-globulin labeled with 1-131 were dissociated into half molecules by reduction and acidification. When a mixture of the two preparations was neutralized, a large proportion of mixed molecules having active combining sites and the same sedimentation coefficient as the original gamma-globulins was formed. Since the sulfhydryl groups were inactivated after reduction, the recombined subunits appear to be linked by noncovalent bonds.

Animals↗

SEROLOGIC DEMONSTRATION OF DUAL SPECIFICITY OF RABBIT BIVALENT HYBRID ANTIBODY.

Hybrid, bivalent antibody molecules bearing specific combining sites for both ovalbumin and bovine gamma globulin were produced by reoxidation of a mixture of the 3.5S fragments of the two specifically purified antibodies. The dual specificity and the properties of the hybrid antibody were demonstrated by mixed agglutination and two stage agglutination experiments, and by test systems utilizing inhibition of agglutination or dispersal of agglutinates followed by antiglobulin reactions.

Agglutination↗

IMMUNOCHEMISTRY.

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Allergy and Immunology↗