Caption: Figure 2: Chemical structure of (a) gliadin, (b) legumin, (c) elastin, and (d) zein.
(2) Size 1-100 nm [8, 9] (3) Polymers Albumin  Gelatin Gliadin Legumin Elastin Soybean Zein Milk protein (4) Formulation (I) Emulsifcation method  Technique (II) Desolvation method (III) Complex coacervation method (IV) Electro-spray method (5) Merits (i) Proteins are able to show [12, 13] better action at minimum dose.
Bovine serum albumin was used to establish the standard curve for the whole albumin fractions, while purified legumin was used for the globulin fractions.
Legumin, vicilin, trypsin inhibitor, and lectin were detected by indirect ELISA in the various chromatographic fractions.
The proteins in Peaks 2 (a and b) and 3 (a and b) corresponded to albumins [PA.sub.2] (MW 26 000) and [PA.sub.1] (MW 11 000), whereas convicilin (MW 71 000), vicilin (main constitutive polypeptides MW ~47 000, 33 000) and legumin ([Alpha] polypeptides MW ~45 000, [Beta] polypeptides MW ~25 000) were eluted in the Peaks 4 (a and b) and 5 (a and b).
ELISA results were consistent with SDS-PAGE patterns; legumin eluted mainly in Peak 5 and vicilin and convicilin eluted in Peak 4 (a and b) (Fig.
Regulation of legumin levels in developing pea seeds under conditions of sulfur deficiency.
Developmental and environmental regulation of pea legumin genes in transgenic tobacco.