Croy R R, Gatehouse J A, Tyler M, Boulter D
Biochem J. 1980 Nov 1;191(2):509-16. doi: 10.1042/bj1910509.
A third storage protein, distinct from legumin and vicilin, has been purified from the seeds of pea (Pisum sativum L.). This protein has been named 'convicilin' and is present in protein bodies isolated from pea seeds. Convicilin has a subunit mol.wt. of 71 000 and a mol.wt. in its native form of 290 000. Convicilin is antigenically dissimilar to legumin, but gives a reaction of identity with vicilin when tested against antibodies raised against both proteins. However, convicilin contains no vicilin subunits and may be clearly separated from vicilin by non-dissociating techniques. Unlike vicilin, convicilin does not interact with concanavalin A, and contains insignificant amounts of carbohydrates. Limited heterogeneity, as shown by isoelectric focusing, N-terminal analysis, and CNBr cleavage, is present in convicilin isolated from a single pea variety; genetic variation of the protein between pea lines has also been observed.
从豌豆（Pisum sativum L.）种子中已纯化出第三种贮藏蛋白，它不同于豆球蛋白和豌豆球蛋白。这种蛋白被命名为“伴豌豆球蛋白”，存在于从豌豆种子中分离出的蛋白体中。伴豌豆球蛋白的亚基分子量为71000，其天然形式的分子量为290000。伴豌豆球蛋白与豆球蛋白在抗原性上不同，但在用针对这两种蛋白产生的抗体进行检测时，与豌豆球蛋白有同一性反应。然而，伴豌豆球蛋白不含豌豆球蛋白亚基，并且可以通过非解离技术与豌豆球蛋白清楚地分离。与豌豆球蛋白不同，伴豌豆球蛋白不与伴刀豆球蛋白A相互作用，并且含有的碳水化合物量极少。从单一豌豆品种中分离出的伴豌豆球蛋白存在有限的异质性，如通过等电聚焦、N端分析和溴化氰裂解所显示的；在豌豆品系之间也观察到了该蛋白的遗传变异。
