ISSN:
1432-0614
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Summary Polyclonal anti-myoglobin antibodies were fractionated into five subpopulations directed against five specific antigenic sites, respectively. The equilibrium characteristics of each subpopulation and orginal anti-myoglobin immobilized to CNBr-activated Sepharose 4B were compared. The four subpopulations of antibodies lost their binding abilities at around pH 4.5 because of the conformational changes of myoglobin. However, the subpopulation directed against the region containing three histidine residues dissociated with the antigenic site at higher pH, and such equilibrium characteristics were considered to be caused by the dissociation characteristics of histidine residues. Therefore, the effects of histidine modification in BSA on the adsorption capacities of original anti-BSA antibody and a pH sensitive fraction of it were compared. The adsorption capacity of the pH sensitive fraction showed greater decrease than that of original antibody by histidine modification in BSA. These results imply that the antigenic sites in which histidine residues play an important role for the binding to antibodies show equilibrium characteristics sensitive to pH.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00451626
