Estudo quimiotaxonômico de sementes de espécies de Mimosoideae (Leguminosae)

Detalhes bibliográficos
Ano de defesa: 1994
Autor(a) principal: Nunes, Edson Paula
Orientador(a): Não Informado pela instituição
Banca de defesa: Não Informado pela instituição
Tipo de documento: Dissertação
Tipo de acesso: Acesso aberto
Idioma: por
Instituição de defesa: Não Informado pela instituição
Programa de Pós-Graduação: Não Informado pela instituição
Departamento: Não Informado pela instituição
País: Não Informado pela instituição
Palavras-chave em Português:
Link de acesso: http://www.repositorio.ufc.br/handle/riufc/46909
Resumo: The content and fatty acid composition of seed lipids in 8 species from the Mimosoideae were analysed. The species investigated belong to 4 Tribes: Acacieae (Acacia farnesiana e A. langsdorffii), Ingeae (Chloroleucon foliolosum e Pithecellobium dulce), Mimoseae (Stryphnodendron coriaceum e S. rotundifolium ) e Parkieae (Parkieae pendula e P. platycephala). In addition, the soluble protein content, the hemagglutinating activity, and the protein electrophoretic pattern of the seeds from these species were also determined. In relation to the seed lipids, the results showed that the fatty acid composition and their ratios may be useful as taxonomic markers for the differentiation of genera belonging to different Tribes of the Mimosoideae, as well as for discrimination of species from the sarne genus. On the other hand, it was not found any taxonomic correlation for the occurence of hemagglutinating activity in the seeds of the 8 species investigated at the Tribe leveI. However, the presence of hemagglutinating activity (or hemolysis) as well as its specificity, that is, the type of erythrocytes agglutinated (or hemolysed), proved to be useful for the discrimination of species from the same genus. The analysis of the electrophoretic profile of the seed proteins showed, in all the species examined, the presence of 2 major groups of protein bands: one group that comprises high molecular weight proteins with mobility similar to that observed for the purified lectin from Parkia platycephala (60 KDa), and a second one constituted of low molecular weight proteins. However, each species exhibited a unique protein pattern that promptly differentiated it from the others.