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Determination of the protein content and amino acid composition of finger millet samples from white-grain and brown-grain varieties, revealed wide variations in protein and amino acid composition. Solubility fractionation of proteins showed that prolamin and glutelin constitute the major protein fractions. Whitegrain varieties have higher prolamin and lower glutelin levels than the brown-grain varieties. The amino acid composition of three protein fractions of one white and one brown variety are reported. These studies suggest that it should be possible to provide hjgh amounts of good quality protein in lines developed from white x brown seed crosses.

A B S T R A C TStudies on the proteins offive varieties of kodo millet showed that there are hardly any varietal differences. Fractionation of the proteins showed that glutelin is the major storage protein. The amino acid compositions of the protein of the five varities of kodo millet and the individual protein fractions of two varieties were determined. Lysine is the most limiting amino acid followed by methionine and cystine. There is no significant negative correlation between lysine levels and protein content. Sodium dodecylsulphate polyacrylamide gel electrophoresis patterns indicate great similarities in the different varieties.

Total protein from five varieties of Japanese barnyard millet (Echinochloa frumentacea) was separated into albuminlglobulin, prolamin and glutelin fractions. The protein fractions were examined by sodium dodecylsulphate polyacrylamide gel electrophoresis. Total protein of the varieties ranged from 110.5 to 139.3 mg g-I of which 11.3-17-2% was albumin/globulins, 6.8-9.3% prolamins, 7.5-11.6% prolamin-like, 5.9-9.1 % glutelin-like and 39-3-54.4% true glutelins. Amino acid analyses of the total protein showed that the varieties had essentially the same amino acid composition. With the exception of lysine the amino acid levels adequately matched the provisional FA0 scoring pattern. The amino acid composition of the protein fractions was also very similar. Electrophoretic analysis showed that the albumin/globulin fraction contained three or four components; the prolamin and glutelin fractions each had five components. The glutelin fraction had higher molecular weight components than the other two fractions.

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