Isolation and characterization of a 20 kD prolamin from kodo millet (Paspalum scrobiculatum) (L.): homology with other millets and cereals.

The homologus 20 kD prolamin from kodo millet and other minor millets viz. barnyard, little and foxtail millets, were purified using preparative gel electrophoresis and reversed phase high performance liquid chromatography (RP-HPLC). The amino acid composition of the purified 20 kD prolamin protein from different minor millets revealed higher content of glutamic acid, alanine, leucine and serine and lower quantity of lysine and methionine. They contain 55 to 58 percent of non-polar amino acids which make them more hydrophobic than other protein fractions. The total number of amino acid residues per polypeptide chain ranged from 152 to 155 based on theoretical calculation. Peptide mapping of the 20 kD prolamin hydrolyzed with trypsin gave fewer cleavage products than expected. The antigenic relationships among these minor millets and cereals viz. wheat, maize, rice, sorghum, finger millet and pearl millet were studied using the antibody raised against the 20 kD prolamin. Cross reactivity was seen in all the minor millets at the 20 kD region. But in barnyard and little millets lower molecular weight polypeptides also cross reacted with the antibody. Immunoblotting studies revealed that the prolamins from other cereals and millets are related to the 20 kD prolamin of kodo millet. Rice was the only common cereal that did not cross react immunologically with the antibody raised against 20 kD prolamin of kodo millet.