Kummer H, Rüdiger H
Institut für Pharmazie und Lebensmittelchemie der Universität Würzburg.
Biol Chem Hoppe Seyler. 1988 Aug;369(8):639-46. doi: 10.1515/bchm3.1988.369.2.639.
From the storage proteins of the pea (Pisum sativum), the fraction which interacts with the pea lectin by the sugar-binding site was studied. By electrophoretical subunit patterns and other criteria, this fraction resembles the group of the 7S storage proteins (vicilins). The fraction was resolved into subunits by micropreparative SDS PAGE. The N-terminal sequences of the individual subunits were determined. Most of these are identical with published vivilin subunit sequences; therefore this lectin-binding fraction belongs to the vicilins. Selected subunits and tryptic fragments were analysed for amino-acid compositions. Though unequivocal assignments to vicilin segments were possible, significant differences could be recognized, in particular in the tryptic fragments.
对豌豆（Pisum sativum）的贮藏蛋白中通过糖结合位点与豌豆凝集素相互作用的部分进行了研究。通过电泳亚基图谱和其他标准，该部分类似于7S贮藏蛋白（豌豆球蛋白）组。通过微量制备SDS-PAGE将该部分分离成亚基。测定了各个亚基的N端序列。其中大部分与已发表的豌豆球蛋白亚基序列相同；因此，这个凝集素结合部分属于豌豆球蛋白。对选定的亚基和胰蛋白酶片段进行了氨基酸组成分析。虽然可以明确地将其归为豌豆球蛋白片段，但也发现了显著差异，特别是在胰蛋白酶片段中。
