The buffer extractable proteins of pea, albumins and globulins, were s
uccessively extracted in a large amount at a pilot scale. In order to
preserve as much as possible the native structure of proteins, a selec
tive solubilization step procedure was performed. Firstly, albumins we
re extracted with acetate buffer and secondly globulins with phosphate
buffer of high ionic strength. Each extract was desalted by diafiltra
tion without protein precipitation. From 15 kg of flour, 380 g of albu
min fraction and 1000 g of globulin fraction were obtained with a prot
ein content of 86.0% and 90.7% of dry matter respectively. The charact
erisation of albumin and globulin fractions by electrophoresis, ultrac
entrifugation and anion-exchange chromatography, showed that the cross
-contamination of these two fractions was minimal.