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• W2069971951 abstract "The Fd-CNBr fragment of anti-4-azo-1-naphthalene sulfonate antibody was obtained by CNBr cleavage of the separated heavy chain of specifically purified rabbit antibody in 0·3 M hydrochloric acid. The Fd-CNBr fragment showed specific binding activity for the hapten, 4-anilinonaphthalene-1-sulfonate (4,1-ANS), as evidenced by an enhancement in the fluorescence of the ligand as occurs when the ligand is bound by specific antibody. The fluorescence enhancement behavior with the Fd-CNBr fragment on serial addition of 4,1-ANS was different from the behavior with the intact or reassociated antibody molecule. There was a much more gradual increment of fluorescence, as expected for much weaker binding, similar to the behavior with light chains. The average binding constant of this fragment with 4,1-ANS was in the order of 103 1/M. Since there was no apparent increase in the fluorescence by the addition of homologous light chains, above that due to the added light chains it appears that the Fd-CNBr fragment does not associate strongly with light chains in contrast to the association of the Fd-papain fragment with light chains." @default.
• W2069971951 created "2016-06-24" @default.
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• W2069971951 date "1975-04-01" @default.
• W2069971951 modified "2023-09-26" @default.
• W2069971951 title "Antibody-ligand interaction studied by fluorescence enhancement method—IV: Hapten binding activity of peptide fragments from purified antibody heavy chain cleaved by cyanogen bromide" @default.
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• W2069971951 doi "https://doi.org/10.1016/0019-2791(75)90182-2" @default.
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