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The purification and characterization of 2 groups of storage proteins secalins from rye secale cereale cultivar reidol



The purification and characterization of 2 groups of storage proteins secalins from rye secale cereale cultivar reidol



Journal of Experimental Botany 33(133): 261-268



Two groups of polypeptides, which together represented > 90% of the secalin fraction, were purified by ion exchange chromatography and gel filtration. These fractions had MW of 40,000 and 75,000 by SDS-PAGE [sodium dodecylsulfate polyacrylamide gel electrophoresis] and 33,000 and 54,000 by sedimentation equilibrium ultracentrifugation, respectively. Isoelectric focusing showed that each fraction contained a number of polypeptides. Amino acid analysis showed that the 2-groups had similar compositions with high glutamate + glutamine and proline and low lysine. The N-terminal sequences of the 2 groups were identical at 17 of the first 20 positions and were similar to those reported for .gamma.2 and .gamma.3-gliadins of wheat. Both groups had C-terminal histidine. Prolamin evolution and homology in barley, rye and wheat is discussed.

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Accession: 006744455

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