The efect of pH and ionic strength on the association and dissociation phenomena of pea 11.9-type globulin (legumin) was investigated. I t was shown by ultracentrijigation and HPLC that the native conformation was maintained only in the pH range 7 to 9. At extreme acidic or basic pH most of the molecules were dissociated. Below pH 3.4 the 12s native form was completely dissociated, and at pH 2.4 only very slow sedimenting components (3.5s) were observed. At low ionic strength aggregation usually occurred.These results were confirmed by U V diference spectroscopy, and it was observed that acidic conditions induced a drastic dissociation of legumin leading to completely unfolded subunits. In this conformation all the tyrosine and tryptophan residues were exposed as shown by second derivative spectra. This spectroscopic study led also to hypotheses on the native structure of legumin and especially on the respective positions of the basic and acidic polypeptides.
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