The polypeptide composition of low molecular weight glutenin (LMWGn) described by Beckwith et al.⁽⁴⁾ was compared with that of the usual glutenin (Gn). Starch gel electrophoresis of reduced and cyanoethylated glutenin (SCE-Gn) and low molecular weight glutenin (SCE-LMWGn) showed that SCE-LMWGn lacked a few components of SCE-Gn. While SCE-Gn was separated into three fractions by gel filtration on Sephadex G-100 column, SCE-LMWGn lacked the second fraction in the same fractionation. The second fraction of SCE-Gn gave three main bands in starch gel electrophoresis. The same components were found in the preciptate when the fractionation of SCE-Gn was made in neutral 70% ethanol. On the other hand, starch gel electrophoretic pattern of the supernatant was similar to that of SCE-LMWGn, which gave no precipitate in neutral 70% ethanol at room temperature. Isoelectric focusing revealed another difference between SCE-Gn and SCE-LMWGn; the latter lacked all of the components of SCE-Gn having isoelectric points lower than 6.4. These lacked components were found in the neutral 70% ethanol insoluble fraction of SCE-Gn and in the first fraction of gel filtration. The components of the second fraction in gel filtration showed isoelectric points higher than 6.4.