Two Groups of Low Molecular Weight Hydrophobic Proteins from Barley Endosperm

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Abstract
The fraction under 25 000 molecular weight from the chloroform-methanol 2: 1 (v/v) extract of barley endosperm contains two different groups of hydrophobic proteins. One group consists of the four major components of the low molecular weight fraction present in hordein preparations (A-hordeins). It is shown that their amino acid compositions are outside the range of typical prolamins and that therefore their designation as A-hordeins is inappropriate. Their chemical characteristics closely resemble those of the wheat CM proteins, which are also salt-soluble and hydrophobic. Components of the second group have high isoelectric points (>pH 9.0), molecular weights in the range 10 000–16 000, and amino acid compositions within the definition of prolamins. They seem to be equivalent to the low molecular weight gliadins from wheat, so it is suggested that they be designated low molecular weight hordeins.