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Lysozyme-binding antibody

Fig. 3. Affinity analysis of wild-type and mutant K49VlcT of MAb HyHEHO sequentially saturated with duck lysozyme in the particle affinity assay. The abscissa (R ) is the corrected proportion of antibody binding sites filled with soluble lysozyme, and the ordinate is equivalent to [Ab] times B/F, as described in the text (Reproduced from Lavoie et al.26)... Fig. 3. Affinity analysis of wild-type and mutant K49VlcT of MAb HyHEHO sequentially saturated with duck lysozyme in the particle affinity assay. The abscissa (R ) is the corrected proportion of antibody binding sites filled with soluble lysozyme, and the ordinate is equivalent to [Ab] times B/F, as described in the text (Reproduced from Lavoie et al.26)...
The conformational energy calculations received support subsequently from two types of experimental study by Smith-Gill et al. (1984). The affinity of ring-necked pheasant lysozyme, in which Asn and Arg at positions 113 and 114 are replaced by Lys and His, respectively, is the same for (NAG)e as that of domestic hen egg-white lysozyme (i.e., the right side is not involved). They also showed that a monoclonal antibody bind-... [Pg.202]

How do large antigens interact with antibodies A large collection of antibod ies raised against hen egg-white lysozyme has been structurally characterized in great detail (Figure 33.15). Each different antibody binds to a distinct... [Pg.954]

The shape of the interaction area between lysozyme and the CDR loops of the antibody is easily distinguished from the hapten-binding crevice. The interaction extends over a large area with maximum dimensions of about 20 X 30 A (Figure 15.15). The interaction surface is irregular but relatively flat, with small protuberances and depressions that are complementary in the antigen and the antibody. Residues from all six CDR loops contribute to the... [Pg.309]

FIGURE 1.12 Van der Waals packing is enhanced in molecules that are structurally complementary. Gln represents a surface protuberance on the protein lysozyme. This protuberance fits nicely within a pocket (formed by Tyr , Tyr , Phe and Trp ) in the antigen-binding domain of an antibody raised against lysozyme. (See also Figure 1.16.)... [Pg.15]

Tsumoto, K., K. Ogasahara, Y. Ueda, K. Watanabe, K. Yutani, and I. Kumagai. 1995. Role of Tyr residues in the contact region of anti-lysozyme monoclonal antibody HyHELlO for antigen binding. J Biol Chem 270 18551-18557. [Pg.379]

Hawkins RE, Russell SJ, Baier M, Winter G, The contribution of contact and noncontact residues of antibody in the affinity of binding to antigen. The interaction of mutant D1.3 antibodies with lysozyme, J. Mol. Biol., 234 958-964, 1993. [Pg.468]


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Lysozyme

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