The free energy of angular position of the fab arms of IgG antibody

Schumaker, Verne N.; Seegan, George W.; Smith, Carr J.; Ma, Shanyun; Rodwell, John D.; Schumaker, M.F

doi:10.1016/0161-5890(80)90063-2

Cited by 39 publications

(21 citation statements)

References 16 publications

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“…Electron microscopy has been previously employed in several studies of Ag-Ab complexes. Early work (36,38) involved studies of anti-hapten complexes. More recently, EM has been used in studies of Fc-mediated precipitation (39), the segmental flexibility of Fab arms (40), and idiotope mapping (41).…”

Section: Discussionmentioning

confidence: 99%

Size and structure of antigen-antibody complexes. Electron microscopy and light scattering studies

Murphy

Slayter

Schurtenberger

et al. 1988

Biophysical Journal

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Size parameters of model antigen-antibody (Ag-Ab) complexes formed by the interaction of bovine serum albumin (BSA) and pairs of monoclonal anti-BSA antibodies (mAb) were evaluated by quasielastic light scattering, classical light scattering, and electron microscopy (EM). Mean values for the hydrodynamic radius, radius of gyration, and molecular weight were determined by light scattering. Detailed information regarding the molecular weight distribution and the presence of cycles or open chains was obtained with EM. Average molecular weights were calculated from the EM data, and the Porod-Kratky wormlike chain theory was used to model the conformational behavior of the Ag-mAb complexes. Ag-mAb complexes prepared from three different mAb pairs displayed significantly different properties as assessed by each of the techniques employed. Observations and size parameter calculations from EM photomicrographs were consistent with the results from light scattering. The differences observed between the mab pairs would not have been predicted by idealized thermodynamic models. These results suggest that the geometric constraints imposed by the individual epitope environment and/or the relative epitope location are important in determining the average size of complexes and the ratio of linear to cyclic complexes.

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Section: Discussionmentioning

confidence: 99%

Size and structure of antigen-antibody complexes. Electron microscopy and light scattering studies

Murphy

Slayter

Schurtenberger

et al. 1988

Biophysical Journal

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“…Apparently the release of the hinge disulphide link between the heavy chains (which is known to occur at mild reduction conditions such as used here [20]) allows the antibody to relax back into a closed Y configuration. This interpretation is supported by the observation that, in multimer formation through a divalent hapten, mild reduction followed by alkylation resulted in an increase of dimers and trimers at the expense of the higher multimers [12].…”

Section: Fgpementioning

confidence: 72%

“…If so, such global configurational changes may contribute to the effect observed with polarization spectroscopy. We would also expect that, in antibody multimer formation studies [12], the multimer distribution would be shifted to low multimers by lowering the pH below 7, and that mouse IgG2. and IgG2b would form predominantly low multimers regardless of pH.…”

Section: Fgpementioning

confidence: 99%

“…the strong tendency to form hexagonal lattices at low as well as high pH is lost with the addition of dithiothreitol (DTT), but no ordering into a different lattice was observed. Previous electron microscopy studies [11,12] of antibody multimer formation induced by divalent haptens indicated that a variety of angles between the Fab arms are possible, and at pH 7.4 the Fab arms appear to be freely flexible and can sample freely Fab-Fab angles between 60°and 180°, the fully extended form. Only in the instance of dimer formation, in which the Fab arm angle is 00, was there an indication of a small strain energy barrier.…”

Section: Introduction Two-dimensional (2-d) Self-organization Of Protmentioning

confidence: 99%

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Antibody organization on lipid films. Influence of pH and interchain disulphide reduction

Uzgiris¹

1990

Biochemical Journal

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Two distinct lattice structures are observed for two-dimensional (2-D) antibody organization on phospholipid films. A low-order, small-unit-cell, square lattice is obtained at pH 7 and below for mouse IgE, mouse IgG2a and IgG2b and rabbit IgG. At pH 7.5 and above, the observed lattice structure switches to a large-unit-cell, hexagonal type for rabbit IgG and mouse IgE. Interchain disulphide reduction by exposure to 2 mM-dithiothreitol results in the formation of the compact 2-D lattice for all cases and for all pH conditions.

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“…derived by Schumaker et al ( 1980). The factor p = 0.6 nm-3 M-1 has to be inserted in order to take into account the particle density in the standard state.…”

Section: Kinetics Of Ige-ring Closurementioning

confidence: 99%

Dimerization kinetics of the IgE-class antibodies by divalent haptens. II. The interactions between intact IgE and haptens

Schweitzer‐Stenner¹,

Licht²,

Pecht³

1992

Biophysical Journal

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Interactions between a monoclonal, DNP-specific IgE molecules (hybridoma A2) and divalent DNP-haptens in solution cause aggregation of the former predominantly into closed rings of two IgE and two divalent haptens (Schweitzer-Stenner, R., A. Licht, I. Lüscher, and I. Pecht. 1987. Biochemistry. 26:3602-3612). The time course of this process was now investigated by titrating the A2-IgE with divalent DNP-haptens having long and rigid oligoproline spacers (di(N epsilon-2,4-dinitrophenyl)-6-amino-hexanoate-aspartyl-(prolyl)n-L-ly- syl; n = 24, 27, 33). Binding was expressed in quenching of the IgE intrinsic tryptophan emission. As shown in the preceding paper, hapten addition to the IgE-A2 at rates faster than a distinct threshold value led to nonequilibrium titrations (NETs) from which kinetic processes slower than 2 s-1 can be resolved. Analysis of these titrations shows that the dimeric rings open at rates of approximately 10(-2) s-1, independent of the divalent hapten's spacer length. The ring closure rate, however, decreases with spacer length. The latter observation was qualitatively rationalized in terms of the diffusion process of a Gaussian chain which relates the ring closure rate constant to the expectation value for the distance between the free ends of the respective open chain.

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The free energy of angular position of the fab arms of IgG antibody

Cited by 39 publications

References 16 publications

Size and structure of antigen-antibody complexes. Electron microscopy and light scattering studies

Size and structure of antigen-antibody complexes. Electron microscopy and light scattering studies

Antibody organization on lipid films. Influence of pH and interchain disulphide reduction

Dimerization kinetics of the IgE-class antibodies by divalent haptens. II. The interactions between intact IgE and haptens

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