The biological effects of heating and chemical treatment on castor meal were investigated in order to develop a procedure to inactivate its antigenic activity in a way that is suitable for industrial applications. A 1% solution of purified castor bean allergen (CB-1A) was heat-treated with or without exposure to NaOH and NaOCI (250 ppm each). CB-1A exhibited extreme stability when heat-treated alone. In the presence of NaOH and NaOCl, CB-1A showed a drastic decrease in antigenic activity as the temperature surpassed the critical level of $70^{circ}C$. The gradual disappearance of disc gel electrophoresis bands presumably responsible for the allergenicity of CB-1A, along with the significant losses of the amino acids phenylalanine, methionine, arginine, histidine, and cysteine correlated with the loss of CB-1A activity. CB-1A showed a single symmetrical band in SDS acrylamide gel electrophoresis with an estimated molecular weight of 6,000 daltons. The chemical and heat treatments reduced the disulfide bond content of CB-1A by 9.1% with a coincident increase in sulfhydryl bonds.