The storage proteins and lectins that accumulate in the protein bodies of developing legume cotyledons undergo a number of processing steps along the transport pathway from their site of synthesis to their site of deposition. The polypeptides are synthesized on polysomes attached to the endoplasmic reticulum. Synthesis of the polypeptides is always accompanied by the co-translational removal of a signal peptide. Those proteins that are glycoproteins in their mature form are co-translationally glycosylated with high-mannose oligosaccharide side chains. Co-translational sequestration into the lumen of the endoplasmic reticulum is followed by the formation of oligomers. Transport of these oligomers to the Golgi complex may occur via tubular connections between the endoplasmic reticulum and the Golgi. In the Golgi complex some of the high-mannose side chains are modified by the removal of five to six mannosyl residues, and the addition of fucosyl and terminal N-acetylglucosaminyl residues. This phenomenon has so far been observed only for phytohaemagglutinin, the lectin of Phaseolus vulgaris. From the Golgi complex the storage proteins and lectins are transported to the protein bodies. This transport is mediated by small electron-dense vesicles. In the protein bodies two types of processing occur: proteolytic processing resulting in the formation of smaller polypeptides, and glycolytic processing resulting in the removal of the terminal N-acetylglucosaminyl residues from the modified carbohydrate side chains. All storage proteins and lectins undergo some of these processing steps, and specific examples are discussed in this paper.