Abstract
Zein was resolved into several components by electrophoresis on polyacrylamide gel in the presence of sodium dodecylsulfate (SDS). Treated with 2-mercaptoethanol (2-ME) in advance, zein wasresolved into only two components by the electrophoresis. These two components were tentatively named α- and β-zein. Both were isolated by gel filtration on Sephacryl S-200 in the presence of SDS and 2-ME. Amino acid analysis showed that a- and β-zein were similar to each other, except that the number of methionine residue was three in the former and one in the latter. Whenprotein bodies isolated from corn endosperms were subjected to electrophoretical analysis, the same characteristics as those found in zein were observed.
