AFFINITY PURIFICATION OF LATEX ANTIGENS

Latex extracts are complex mixtures of antigenic peptides. We attempte d to raise monoclonal antibodies to latex and to use these antibodies to purify latex antigens. A monoclonal antibody, CRI-C, was raised by standard techniques. Peptides of nonammoniated latex (NAL) and ammonia ted latex were electrophoretically separated and transferred for immun oblots. CRI-C was covalently attached to an agarose column. NAL was pa ssed over the column, and purified antigen was then eluted. The eluate was analyzed by sodium dodecylsulfate-polyacrylamide gel electrophore sis and RAST inhibition with sera from health care workers and childre n with spina bifida. CRI-C recognized a single band in ammoniated late x immunoblots and several distinct bands in NAL. The affinity-purified antigen of CRI-C (C-Ag) had multiple bands of less than 20 kd and was 3.9 times more potent in RAST inhibition than NAL when sera from pati ents with spina bifida were used However, when health care workers' se ra were used, there was no significant difference in the inhibitory po tency of NAL and C-Ag. CRI-C appears to recognize a distinct and impor tant epitope in the IgE immune response to latex of patients with spin a bifida.