Interaction of phytate with mustard 12S protein

Abstract

Binding of phytic acid with the mustard 12S protein was studied in the pH range 5.0-1.0 by the techniques of precipitation, turbidimetry, electrophoresis, and electrometric titration. The binding increased with decreasing pH. At pH 3.0, max. binding of 170 mol of P/mol of protein was observed, which agreed with the basic amino acid content of the protein. Only one class of binding sites was indicated. Electrophoretic studies indicated that even at pH 3.0 some amount of protein was still left in solution. Electrometric titration studies indicated the possibility of the presence of soluble protein-phytate complexes in the system. At pH 3.0, Ca inhibited the formation of protein-phytate complex.