Preparations of total human casein and its individual fractions were isolated for production of specific polyclonal antibodies. Immunization procedures used differed in the schedule for antigen administration, antigen concentrations, degree of additional purification, and modification of the size of molecules. Immunoprecipitation techniques failed to provide an unambiguous proof of the presence of antibodies to human milk caseins in antisera even after immunization of animals phylogenetically considerably different from man. Immunoblotting, however, allowed antibodies to beta-casein to be identified and compared with available monoclonal antibodies.
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