Abstract
The aim of the present work was to investigate the homology of seed storage proteins in a wide variety of conifers for most of which the gene sequences are not yet identified. Rabbit antiserum antibodies against the purified 57 kDa non-reduced crystalloid protein complex of white spruce seed were obtained. The antibodies were used in the immunoblot assays with seed proteins of various members of Pinaceae; Ginkgo biloba, and several representatives of angiosperms. Under reducing conditions, 35 kDa and 22 kDa range polypeptides, homologous to white spruce crystalloids, were identified in all members of the Pinaceae examined except Abies amabilis and Tsuga heterophylla
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