Abstract:
:The interaction between a single-chain Fv (sFv) of the monoclonal antibody 3A21 and its antigen, bovine pancreatic ribonuclease A (RNase A), was studied by site-directed mutagenesis of the hypervariable regions and fluorescence polarization analysis. The affinity constants of wild-type sFv and a mutant sFv D31A (Asp31 of heavy chain was replaced by Ala) for RNase A were found to be 2.7 x 10(7) and 4.7 x 10(6) M-1 in PBS at pH 7.2 and 37 degrees C, respectively. While the affinity constant of D31A is not affected by NaCl concentration, that of wild-type sFv is almost the same as that of D31A in the presence of more than 1 M NaCl. These results demonstrate that Asp31 of the heavy chain interacts electrostatically with a positively charged amino acid residue of RNase A.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Katakura Y,Kumamoto T,Iwai Y,Kurokawa Y,Omasa T,Suga Kdoi
10.1016/s0161-5890(97)00094-1subject
Has Abstractpub_date
1997-07-01 00:00:00pages
731-4issue
10eissn
0161-5890issn
1872-9142pii
S0161589097000941journal_volume
34pub_type
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