Abstract
Like Brassica napus L. cv. Darmor (rapeseed) cruciferin, the seed 11S globulin of diploid species, B. oleracea L. cv. Valentine (cauliflower) and cv. Proteor (fodder cabbage) and B. campestris L. cv. Chicon (fodder turnip), had legumin-like subunit consisting in large (αs) and small (βs) disulfide-linked polypeptide components and, in addition, α and β free (f) polypeptides not covalently bonded. Free and subunit component polypeptides of the 11S cruciferin from different species were compared using two dimensional gel electrophoresis analysis, CNBr and V8 protease peptide mapping experiments and immunological studies. It has been established that (i) αf and αs polypeptides had high degree of homology. (ii) βs polypeptides were similar. (iii) βf polypeptides were different, not only from βs polypeptides but also between them. (iv) In spite of these differences, the βf and βs polypeptides were immunologically related as were the αf and αs polypeptides.
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