The effect of alkaline pH on the association, dissociation, and denaturation of carmin, the high-molecular-weight protein from safflower seed was investigated in the pH range 7-12, using various biophysical techniques. The results indicate that the multimeric protein carmin dissociates at pH 8.0 where denaturation has not set in. The association-dissociation of the protein can be represented schematically as 11S in equilibrium 7S in equilibrium 4S----2S. Above pH 10, the protein undergoes simultaneous dissociation and denaturation. The denaturation process appears to be complete at approximately pH 12.5. The protein undergoes conformational change and covalent modifications and cleavage during the denaturation process. A reversibility study shows that the process of dissociation is reversible to a large extent, whereas denaturation appears to be irreversible. These results are discussed in terms of association-dissociation, denaturation and alkaline-catalyzed covalent modifications and cleavage of seed proteins.