Differences in the Chemical Composition of Some Pea Proteins.

Publisher Website
Google Scholar
Abstract
The proteins vicilin, legumin, and albumin of the pea, Pisum. sativium. were separated and analyzed. The fractions of each protein were examined in the ultracentrifuge in order to show relative purity, and these studies showed that vicilin and legumin were 2 different protein components, not products formed in situ during purification. Vicilin and legumin did not differ appreciably in N content nor in the tyrosine content; but legumin contained much more tryptophan. The distribution of acid, neutral, and basic amino acids among the pea proteins was determined. These studies added to electrophoretic results showed that vicilin and legumin are 2 well-defined globulins. The high content of tryptophan and of lysine in the albumin fraction was remarkable and reminiscent of the values found in animal proteins, e.g., beta-lactoglobulin.