Ferritins from maize, pea, and soya bean seeds were purified. They contain two polypeptides of 28 and 26.5 kDa. The molecular weight of native pea seed ferritin has been estimated to be 540,000. Pea and maize seed ferritins were compared by reverse phase high performance liquid chromatography, amino acid composition, and two-dimensional gel electrophoresis. They are very similar, although four isoforms of the 28-kDa polypeptide from the pea were observed in contrast to a unique polypeptide in maize. No isoforms of the 26.5-kDa polypeptide were detected. Rabbit antibodies were produced in response to pea seed ferritin. It was shown by Western blot analysis that ferritins of the three plants analyzed share immunological determinants. However, horse spleen ferritin was not recognized by the phytoferritin antibodies. Antibodies were also used to demonstrate that ferritins are not uniformly distributed in different pea organs from 30-day-old iron-unloaded plants. The protein was more abundant in flowers than in fruits and roots, and was not detected in leaves.