Separation of univalent fragments of rabbit antibody by reduction of a single, labile disulphide bond.
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Animals↗
Biomedical subjects
A NISONOFF
Publications and source records attributed to A NISONOFF.
Recombination of a mixture of univalent antibody fragments of different specificity.
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Antibodies↗
Nature of the active site of antibenzoate antibodies: further evidence for the presence of tyrosine.
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Antibodies↗
Specific anion effects with antibenzoate antibody.
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Anions↗
Recombination of univalent subunits derived from rabbit antibody.
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Animals↗
Properties of the major component of a peptic digest of rabbit antibody.
The molecular weight of the active, major component isolated from a peptic digest of rabbit antibody was found to be 106,000. After treatment with a disulfide-splitting reagent, the molecular weight was 56,000, and the products migrated as a single peak in the ultracentrifuge. he univalent fragments thus formed can be partially recombined by passage through IR-120 cation-exchange resin at room temperature or by treatment with a difunctional organic mercurial. Some splitting of the pepsin-treated antibody molecule occurs on carboxymethylcellulose at pH 5.4.
Animals↗
Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bonds.
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Animals↗
Properties of univalent fragments of rabbit antibody isolated by specific adsorption.
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Adsorption↗
Resynthesis of precipitating antibody from univalent fragments.
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Antibodies↗
Effect of hydrolysis by papain on the combining sites of an antibody.
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Antibodies↗
The similar specificity of the combining sites of an individual antibody molecule.
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Antibodies↗
Loss of precipitating activity of antibody without destruction of binding sites.
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Antibodies↗
Heterogeneity and average combining constants of antibodies from individual rabbits.
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Animals↗
The reaction of chicken ovalbumin with homologous antibody in the region of antibody excess.
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Animals↗
Heterogeneity of antibody sites in their relative combining affinities for structurally related haptens.
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Antibodies↗
Mechanisms in enzymatic transamination reaction between carbon chains of same length.
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Carbon↗
Mechanisms in enzymatic transamination; estimation of velocity of the glutamate-aspartate reaction at equilibrium.
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Aspartic Acid↗
Mechanisms in enzymatic transamination; variables in the spectrophotometric estimation of glutamate-aspartate kinetics.
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Aspartic Acid↗