N-terminal sequences of oat avenins compared to other cereal prolamins.
Like the alcohol-soluble seed storage proteins (also called prolamins) of other cereals, avenins, the oat prolamins, are a series of polymorphic molecules belonging to a multigenic family stored within the protein bodies of the starchy endosperm. Nevertheless, they exhibit some pecularities: among the seed storage proteins, their proportion is low compared to prolamins from other cereal species; their net charge is higher; the amount of Gln + Pro only reaches 49 mol%; they are less polymorphic. We have isolated and purified several avenins and sequenced their N-terminal end. The microheterogeneity and the pecularity of avenins are revealed by the comparison of the N-terminal sequences. Like other prolamins, they exhibit tandem repeats; these repetitive peptides are slightly different from those of other prolamins of the Festucoideae, and the repetition begins earlier in the sequence. As for prolamins from other species, their predicted secondary structure reveals successive beta-turns which might be arranged in a pseudo-helix structure.
D000595:Amino Acid Sequence; D001483:Base Sequence; D002523:Edible Grain / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010940:Plant Proteins / Q000032:analysis* / Q000302:isolation & purification; D055315:Prolamins
D010940:Plant Proteins; D055315:Prolamins