Abstract
Lectins are proteins capable of specific and reversible recognition of
carbohydrates without modifying them. Many studies have isolated these
molecules from Leguminosae seeds but little attention was given to
subcellular localization and biological function of these molecules.
Therefore, this work aimed to describe Canavalia brasiliensis seed
structure and the subcellular localization of ConBr. In addition, we
tested the affinity of anti-ConBr antibody for other lectins. To
accomplish this, seed fragments were processed for light, scanning and
transmission electron microscopy, as well as immunocytochemistry. The
anti-ConBr affinity was also tested. Under SEM, the testa showed a
regular contour of anticlinal walls without trichomes and inner
integument of 10-20 cell layers. The cotyledons presented many
parenchymatic cell layers with starch grains and cytoplasmic protein
bodies. The immunological identity of anti-ConBr immunoglobulin to ConBr
and other lectins was confirmed by immunodiffusion and Western blotting.
Ultrastructurally, the cotyledons showed protein bodies characterized by
heterogeneous appearance of irregularly formed electron-dense and
electron-lucent areas. Immunolocalization showed lectin at both protein
bodies and cell wall, however, more studies are required for the
elucidation of ConBr functions. Moreover, the affinity of anti-ConBr for
different lectins can make this molecule a useful biotechnological tool
for lectin studies. (C) 2015 Elsevier GmbH. All rights reserved.
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