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Antibody-combining site modification

Genetic or chemical modification of the antibody-combining site An introduction and positioning of catalytic residue(s) into antibody combining site can be achieved by ... [Pg.386]

If necessary, these combining sites may be equipped with an appropriately positioned catalytic amino acid side chain or a cofactor, which may be introduced either directly by site-directed mutagenesis or indirectly by chemical modification. Antibodies bind molecules ranging in size from about 6 to 34 A with association constants of M , in other words, binding is extremely strong. As with... [Pg.375]

Information about the putative folding of the H,K-ATPase catalytic subunit through the membrane has been obtained by the combined use of hydropathy analysis according to the criteria of Kyte and Doolittle [51], identification of sites sensitive to chemical modification [46,48,50,52-55], and localization of epitopes of monoclonal antibodies [56]. The model of the H,K-ATPase catalytic subunit (Fig. 1) which has emerged from these studies shows ten transmembrane segments and contains cytosolic N- and C-termini [53]. This secondary structure of the catalytic subunit is probably a common feature of the catalytic subunits of P-type ATPases, since evidence supporting a ten a-helical model with cytosolic N- and C-termini has also been published recently for both Ca-ATPase of the sarcoplasmic reticulum and Na,K-ATPase [57-59]. [Pg.29]


See other pages where Antibody-combining site modification is mentioned: [Pg.312]    [Pg.312]    [Pg.141]    [Pg.24]    [Pg.37]    [Pg.197]    [Pg.438]    [Pg.252]    [Pg.74]    [Pg.74]    [Pg.90]    [Pg.130]    [Pg.246]    [Pg.413]    [Pg.388]    [Pg.130]    [Pg.24]    [Pg.257]    [Pg.97]    [Pg.709]    [Pg.604]    [Pg.41]    [Pg.210]    [Pg.1308]    [Pg.211]    [Pg.314]    [Pg.144]    [Pg.1971]    [Pg.94]    [Pg.584]    [Pg.219]    [Pg.361]    [Pg.461]    [Pg.353]    [Pg.616]    [Pg.667]   
See also in sourсe #XX -- [ Pg.386 ]




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