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Orientador(es)
Resumo(s)
Legume lectins comprise a structurally related, Ca/Mn-dependent, widespread,
abundant and well characterized lectin family when compared to the large number of lectins
from other sources described in the literature. Strangely enough, no specific function has
been assigned to them aside from a possible role in storage and/or defense. Using a recent
and fine-tuned methodology capable of specific lectin identification, β-conglutin, Vicia faba
vicilin and β-lathyrin, the vicilin storage globulins from Lupinus albus, V. faba and
Lathyrus sativus, respectively, were shown to be capable of affinity binding to thoroughly
washed erythrocyte membranes and of specific elution with appropriate sugars. Based on
this evidence and on sparse data published in the literature, a second family of legume
lectins is proposed: the 7S family of storage proteins from leguminous seeds, or family II
of legume lectins. These lectins are also structurally related, widespread and well
characterized. In addition, they self-aggregate in a Ca/Mg, electrostatic dependent manner
and are even more abundant than the family I of legume lectins. Using the same evidence,
reserve and defense roles may be attributed to family II of legume lectins
Descrição
Palavras-chave
globulin glycosylated receptor Lathyrus sativus Lupinus albus seed Vicia faba
Contexto Educativo
Citação
Editora
MDPI
