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Legumin-like storage polypeptides of conifer seeds and their antigenic cross-reactivity with 11S globulins from angiosperms
Santosh Misra and Margaret Green
Journal of Experimental Botany
Vol. 45, No. 271 (FEBRUARY 1994), pp. 269-274
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/23694747
Page Count: 6
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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. In Ginkgo the antibodies cross-reacted with the previously reported legumin-like polypeptides of 28, 20 and 13 kDa range. In angiosperms, the crystalloid antibodies cross-reacted to the 35 kDa and 20 kDa range of 11S storage polypeptides of Brassica napus, Ricinus communis and Nicotiana tabacum. No cross-homology was observed with the polypeptides of Phaseolus vulgaris, Glycine max, Pisum sativum, and Medicago sativa seeds. Based on the antigenic homology the wide occurrence of legumin-like proteins in gymnosperms is confirmed. Also, the pattern of serological reactivity suggests that the legumin-like proteins of gymnosperms are more closely related to members of Euphorbiaceae, Brassicaceae and Solanaceae than to those of the Fabaceae.
Journal of Experimental Botany © 1994 Oxford University Press