Seven rapeseed varieties were characterized by investigation of the patterns of buffer soluble proteins using polyacrylamide gel electrophoresis and high‐performance liquid chromatography (size‐exclusion and cation‐exchange chromatography). Most pronounced differences were found in proteins not belonging to 12 S and 2 S storage proteins having presumably metabolic functions. Quantitative variations dominate within the low molecular mass 2 S storage proteins.
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Raab et al. (1992) studied this question.
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