1973
DOI: 10.1016/0014-5793(73)80310-2
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Spin—spin interaction between iminoxyl radicals localised in antibody combining sites

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Cited by 10 publications
(14 citation statements)
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“…124 This result is in agreement with the concept that the A conformer represents an inflexible state of the immunoglobulins. 107 The proposal was made that the lower segmental flexibility of IgE is caused by an additional bonding between Fab segments which results in their joint rotation around the Fc segment.124 This peculiarity of the IgE structure agrees with the fact that the IgE antibodies do not form a precipitate after combining with the antigen. 124 The carbohydrate group of IgE(Yu) was spin labeled.105…”
Section: Immunoglobulinsmentioning
confidence: 81%
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“…124 This result is in agreement with the concept that the A conformer represents an inflexible state of the immunoglobulins. 107 The proposal was made that the lower segmental flexibility of IgE is caused by an additional bonding between Fab segments which results in their joint rotation around the Fc segment.124 This peculiarity of the IgE structure agrees with the fact that the IgE antibodies do not form a precipitate after combining with the antigen. 124 The carbohydrate group of IgE(Yu) was spin labeled.105…”
Section: Immunoglobulinsmentioning
confidence: 81%
“…125 These results are in contrast to those obtained in experiments in which the spin label was bound to the protein component of the IgG antibody.107"109 For example, antibodies spin labeled on protein with either 35 or 7b were prepared against immunoglobulins or other substances. 107 The ESR spectra of the resulting complexes between labeled antibodies and antigens indicated an increase in the less mobile A conformer. 107 The rc values of the spin label increased, corresponding to a decreased rotational mobility of the label attached to the protein of the Fab segment.…”
Section: Immunoglobulinsmentioning
confidence: 97%
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