Protein deposit and protein body formation in the seed of the yellow lupin were observed by optical microscopy for different stages of maturation. At the same time, storage protein biosynthesis was assessed by study of polypeptide composition of whole proteins and purified fractions, through electrophoresis and by the use of 2 specific sera. Conglutin gamma was synthesized from 22 DAA (day after anthesis) prior to protein deposition in the vacuoles. During the period of intense synthetic activity in the seed (27-33 DAA), mature forms of conglutins alpha (legumin) and delta (2S fraction) appeared. Two types of protein bodies were detected depending on whether the matrices were homogeneous or heterogeneous. No conglutin gamma precursor could be detected by serum anti-conglutin gamma. Polypeptides of 84, 74 and 62 kDa present at 27 DAA were recognized by serum anti-conglutin alpha, suggesting that the biosynthetic process of conglutin alpha was the same in yellow lupin as in other lupins.