Abstract:
:We examined the effects of histidine residues that were artificially introduced into complementarity-determining regions of antibodies on antigen-antibody interactions at different pH values. Using a monoclonal antibody specific for hen egg-white lysozyme and three mutant antibodies that contained a histidine residue, we measured binding constants for antibodies and lysozyme at different pH values (pH 5-8). No gross conformational changes were evident over this range of pH values, as determined by analysis of the spectra of circular dichroism. Since the charge on a histidine residue is the most likely factor that can vary over this range of pH values, differences on pH-dependent antigen-binding patterns observed between the wild-type and mutant antibodies should be due mainly to the effects of the charges on the histidine residues. The three mutant antibodies showed different and characteristic patterns of pH-dependent binding to lysozyme, which depended on the location of the artificially introduced histidine residues.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ito W,Sakato N,Fujio H,Yutani K,Arata Y,Kurosawa Ydoi
10.1016/0014-5793(92)80745-3keywords:
subject
Has Abstractpub_date
1992-08-31 00:00:00pages
85-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(92)80745-3journal_volume
309pub_type
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