1969
DOI: 10.1016/0005-2795(69)90099-3
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Conformational studies of immunoglobulin G and its subunits by the methods of hydrogen deuterium exchange and infrared spectroscopy

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Cited by 35 publications
(15 citation statements)
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“…In the present study, the antigen binding activity of human IgG monomers survived acid treatment at pH 3.0-3.5 but the complement binding activity was reduced by the treatment. This phenomenon may correlate with the phenomenon that Fab and F(ab' )2 fragments were more stable than Fc fragment in acidic condition (Abaturov et al 1969;Charlwood and Utsumi 1969).…”
Section: Discussionmentioning
confidence: 66%
“…In the present study, the antigen binding activity of human IgG monomers survived acid treatment at pH 3.0-3.5 but the complement binding activity was reduced by the treatment. This phenomenon may correlate with the phenomenon that Fab and F(ab' )2 fragments were more stable than Fc fragment in acidic condition (Abaturov et al 1969;Charlwood and Utsumi 1969).…”
Section: Discussionmentioning
confidence: 66%
“…Abaturov L. V. et al [54] have reported the observed frequencies of four amide bands of IgG, its peptide chains and proteolytic fragments. The frequencies and the shape of the amide bands of sulfonated IgG and F(ab') 2 fragment were identical to those of the complete molecule.…”
Section: Discussionmentioning
confidence: 99%
“…The rate of hydrogen -deuterium (' H + 2H) exchange in peptide NH groups was monitored by infrared spectroscopy [8] with the use of UR-10 and UR-20 spectrophotometers (Carl Zeiss, Iena, DDR). The exchange reaction was initiated by gel filtration through a short column of Sephadex G-25 (fine), equilibrated with a heavy water buffer.…”
Section: Methodsmentioning
confidence: 99%