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“…The affinity of bispecific mouse IgG2a/IgG2b hybrid antibodies suggests that only one cytophilic H chain is required for the IgGl-FcRI interaction (13). However, the findings that only dimeric isolated CH2 domains are cytophilic (12) and that the CH3 domain-deleted IgGi paraprotein SIZ fails to bind FcXRI (10) infer that quaternary interactions between the domains are required to stabilize the active conformation of the IgG1 effector site. Furthermore, inactive aglycosylated IgG1 displays significantly enhanced sensitivity to pepsin and chymotrypsin (25).…”
Section: Discussionmentioning
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“…The affinity of bispecific mouse IgG2a/IgG2b hybrid antibodies suggests that only one cytophilic H chain is required for the IgGl-FcRI interaction (13). However, the findings that only dimeric isolated CH2 domains are cytophilic (12) and that the CH3 domain-deleted IgGi paraprotein SIZ fails to bind FcXRI (10) infer that quaternary interactions between the domains are required to stabilize the active conformation of the IgG1 effector site. Furthermore, inactive aglycosylated IgG1 displays significantly enhanced sensitivity to pepsin and chymotrypsin (25).…”
Section: Discussionmentioning
“…USA 88 (1991) recognition. Covalent IgG1 CH2 domain dimers retain 85% of the cytophilic activity of the parent molecule (11), whereas the CH2 domain-deleted paraprotein IgG1 TIM is devoid of activity (10). Furthermore, monoclonal anti-CH2 antibodies inhibit the IgG1-FcXRI interaction (9).…”
Section: Discussionmentioning
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“…Similarly, preparations of bovine, ovine and caprine IgG had been found to exhibit no appreciable binding to FcyRl [9]. Recently determined sequences for these IgGs [14,151 indicate deletions or amino acid substitutions within the region of the proposed site, presumably rendering them unable to interact with human FcyRI.…”
Section: Vol 18mentioning