Summary
Variant forms of legumin (one of the major storage globulins of Pisum seeds) were purified by immunoamnity chromatography from a range of Pisum types, including P.fulvum, and primitiveforms, modern cultivars and advanced breeding selections of P. sativum. The purified variants, all of which had sedimentation coefficients of about 12S and leucine, threonine and glycine as N-terminal amino acids, showed subunit heterogeneity on Polyacrylamide gels containing sodium dodecyl sulphate and on two-dimensional isofocusing/electrophoresis. Comparison of legumins from different Pisum types showed variability, both in the net surface charge of the whole molecule and in the nature of subunit heterogeneity on two-dimensional gels. The usefulness of two-dimensional gels in the genetic analysis of pea seed storage protein structure was stressed and the role of potential artefacts in such analyses assessed.
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Acknowledgements
Acknowledgments.-I thank Professor D. R. Davies for constructive discussions and advice, Miss E. Sanger for excellent technical assistance, Mr L. S. Clarke and Mr S. Frey for photography, Mr D. C. Wilton and Mr K. Forster for constructing the micro-scale two-dimensional gel apparatus and Dr A. E. Arthur for advice on statistics.
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Casey, R. Genetic variability in the structure of the α-subunits of legumin from Pisum—a two-dimensional gel electrophoresis study. Heredity 43, 265–272 (1979). https://doi.org/10.1038/hdy.1979.82
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DOI: https://doi.org/10.1038/hdy.1979.82
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