Bacon J R, Lambert N, Phalp M, Plumb G W, Wright D J
Anal Biochem. 1987 Jan;160(1):202-10. doi: 10.1016/0003-2697(87)90631-2.
Pea legumin was dissociated into its component subunits by 6 M urea: these were subsequently fractionated by FPLC using a combination of Mono P, Mono Q, and Mono S columns. The resolution and speed of separation were greatly improved in comparison with previous fractionations. Twelve discrete fractions were obtained and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six "normal" legumin subunits (Mr 60,000) were identified as well as some "large" (Mr 66,000) and "small" (Mr 44,000) subunits. A few polypeptides of unknown origin were also observed. Four subunits were purified to homogeneity as adjudged by electrophoresis and HPLC and in sufficient yields to permit further studies. Anomalous electrophoretic behavior of the legumin subunits was also observed.
豌豆豆球蛋白通过6M尿素解离成其组成亚基：随后使用Mono P、Mono Q和Mono S柱的组合通过快速蛋白质液相色谱（FPLC）对这些亚基进行分级分离。与之前的分级分离相比，分离的分辨率和速度有了很大提高。获得了12个离散级分，并通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳进行分析。鉴定出了6个“正常”豆球蛋白亚基（分子量60,000）以及一些“大”（分子量66,000）和“小”（分子量44,000）亚基。还观察到一些来源不明的多肽。通过电泳和高效液相色谱（HPLC）判断，4个亚基被纯化至同质，且产量足以进行进一步研究。还观察到了豆球蛋白亚基的异常电泳行为。
