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Extraction separation and polymorphism of the prolamin storage proteins secalins of rye



Extraction separation and polymorphism of the prolamin storage proteins secalins of rye



Cereal Chemistry 60(1): 1-6



The amounts of secalin extracted from milled grain of rye with 3 alcohol/water mixtures were compared. Two sequential fractions were extracted with the solvent along (secalin-I) and then with the solvent + 2% (vol/vol) 2-mercaptoethanol (secalin-II). The relative amounts of N recovered in the 2 fractions extracted at 20.degree. C were greatest with 50% propan-1-ol (32.5%) and least with 60% ethanol (24%). The 2 fractions extracted with 50% propan-1-ol at 60.degree. C contained > 40% of the N, although electrophoresis showed some nonsecalin components in the secalin-II. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) or the fractions showed 4 groups of polypeptides called high MW (HMW) secalins, 75,000-dalton .gamma.-secalins, .omega.-secalins and 40,000-dalton .gamma.-secalins. Secalin-II contained mainly HMW secalins and 75,000-dalton .gamma.-secalins. SDS-PAGE of unreduced and reduced secalin-I indicated that the HMW and 75,000-dalton .gamma.-secalins were extracted as disulfide-linked aggregates. Fractions were also separated by electrophoresis at pH 3.2 and by three 2-dimensional procedures. These showed that the 40,000- and 75,000-dalton .gamma.-secalins were complex groups of polypeptides. Analysis of single seeds showed variation in secalin patterns within and between commercial varieties. This was not present in a homozygous population and 2-dimensional analysis of secalin from this line showed a smaller number of components.

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