Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
about
Resonance Raman-spectroscopic studies of the hapten features involved in the binding of 2,4-dinitrophenyl haptens by the mouse myeloma proteins MOPC 315 and MOPC 460The combining site of the dinitrophenyl-binding immunoglobulin A myeloma protein MOPC 315A comparison of the isoelectrofocusing porperties of antibodies to DNP, DNP-glycylglycylglycine and DNP-p-aminobenzoylglutamateN-bromosuccinimide oxidation of anti-DNP and anti-DNP-p-aminobenzoylglutamate antibodies in the presence and absence of protecting haptenDifferences in electrostatic properties at antibody-antigen binding sites: implications for specificity and cross-reactivity.Hapten-linked conformational equilibria in immunolglobulins XRPC-24 and J-539 observed by chemical relaxation.Structure-function relations in phosphorylcholine-binding mouse myeloma proteins.Kinetic evidence for hapten-induced conformational transition in immunoglobin MOPC 460.Activation specificity of arsonate-reactive T cell clones. Structural requirements for hapten recognition and comparison with monoclonal antibodies.Some recent applications of the use of paramagnetic centres to probe biological systems using nuclear magnetic resonance.Interactions of the lanthanide- and hapten-binding sites in the Fv fragment from the myeloma protein MOPC 315.Correlations between three-dimensional structure and function of immunoglobulins.Resonance Raman spectroscopy in biochemistry and biology.Structure of an antibody combining site by magnetic resonance.The gross architecture of an antibody-combining site as determined by spin-label mapping.Thermodynamic and spectroscopic comparison of the binding sites of the mouse myeloma protein 315 and of its light chain dimer.The variability of nitro group--protein interaction in the 2,4-dinitrophenyl-binding antibodies M315, M460 and X25 investigated by resonance Raman spectroscopy.The role of nitro groups in the binding of nitroaromatics to protein MOPC 315.Dimerization kinetics of the IgE-class antibodies by divalent haptens. I. The Fab-hapten interactions.The binding of 2,4,6-trinitrophenyl derivatives to the mouse myeloma immunoglobulin A protein MOPC 315.Specificity of interactions of hapten side chains with the combining site of the myeloma protein MOPC 315.
P2860
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P2860
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
description
1974 nî lūn-bûn
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1974年の論文
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1974年学术文章
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1974年学术文章
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1974年学术文章
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1974年学术文章
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1974年学术文章
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1974年学术文章
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1974年學術文章
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1974年學術文章
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name
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
@en
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
@nl
type
label
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
@en
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
@nl
prefLabel
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
@en
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
@nl
P2093
P356
P1433
P1476
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.
@en
P2093
P304
P356
10.1021/BI00707A030
P407
P577
1974-05-01T00:00:00Z