Zein of maize grain: I--Isolation by gel filtration and characterization of monomeric and dimeric species.

Unreduced zein chromatographed on Sephadex G 200 in 8 M urea, on G 100 in 1.5 or 2.5% sodium dodecyl sulfate (SDS) and on hydroxypropylated G 100 in 70% ethanol was resolved into two minor fractions A and B and two major ones D and M irrespective of the medium. The quantitative importance of the fraction M was dependent on the isolation conditions of zein. It decreased from 53% of the proteins contained in ethanolic extract and chromatographed as they were extracted, to 40% of the purified zein. The molecular weight values obtained from SDS-polyacrylamide gel electrophoresis and amino acid compositional data indicated that fractions D and M, as isolated from purified zein in the presence of ethanol, represented respectively dimeric and monomeric forms of a mixture of Mr 22 000 and 24 000 polypeptides with threonine or phenylalanine as NH2-terminal residue. Electrophoretic analysis of selectively carbamylated fraction M on starch gel at pH 3.5 revealed that zein subunits comprised several polypeptides differing in the number and the nature of basic amino acids. At least one of these polypeptides contained one lysyl residue.