Low molecular weight globulins, which are abundant proteins in the Pinus pinaster Ait. megagametophyte, were purified and characterized. They showed a dimeric structure formed of one large and one small subunit linked by disulfide bridges. They were characterized by a high Arg and Glx content and by a relatively high Cys content. A comparison of their characteristics with those of angiosperm 2S proteins suggests that there is homology between them.