Abstract
Oat (Avena sativa L.) seed globulin was extracted from ground caryopses with 1 M NaCl, 0.05 M Tris(hydroxymethyl)aminoethane (ph 8.5) at room temperature. The globulin had a sedimentation constant of 12.1, and a MW of 322,000, as determined by analytical ultracentrifugation. The globulin could be separated into 2 major subunits by sodium-dodecyl sulfate polyacrylamide gel electrophoresis. MW of the subunits were 21,700 (.alpha.) and 31,700 (.beta.), and they were present in equimolar amounts. A subunit model of 6.alpha. and 6.beta. per molecule of globulin is proposed. Amino acid analysis indicated that the .alpha. subunit contained more basic amino acids and aspartic acid/asparagine but less glutamic acid/glutamine and glycine than the .beta. subunit.