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