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The aim of this study was to investigate the effect of non-enzymatic glycosylation and hydrolysis of pea albumins with pepsin on their immunoreactive properties. Albumin fraction was isolated from pea seeds an then glycated and hydrolysed by pepsin. Pea albumin was characterised by SDS‑PAGE and glycotest. A 15% progress in non-enzymatic glycosylation was found. The in vivo experiment demonstrated the influence of glycation on mouse mucosal immune system. The influence of native, glycated and hydrolysed pea albumins on spleen (SPL) and mesenteric lymph nodes (MLN) lymphocytes proliferation was investigated. The culture MLN lymphocytes showed an increase in proliferation during stimulation with all of antigens (native, glycated, hydrolyzed). The proliferation was higher in MLN lymphocyte of the intraperitoneally-sensitized group. This observation suggests that the route of immunization can affect their immunoreactivity. SPL lymphocytes of the orally-immunized group showed higher proliferation as compared with SPL lymphocytes of the group sensitized before oral immunization. It is likely that the route of antigen administration has induced a specific food tolerance. The results suggest that none of the modifications performed has changed the immunoreactivity of the investigated proteins to a great extent.
Plant growth throughout the world is often limited by unfavourable environmental conditions. This paper reports results of a study on long- and short-term osmotic stress (−0.5 MPa) followed by a recovery on in vitro translational capacity of polysomes and on the composition of polysome-associated proteins in germinating pea (Pisum sativum L.) seeds. Here we show that, under osmotic stress, cytoskeleton-bound polysomes were charaterized by the highest translation activity, which may be indicative of an important role that this population of polysomes plays in the synthesis of the so-called “stress proteins”. We also find out that in response to osmotic stress, new proteins (22.01, 96.47 and 105.3 kDa), absent in the unstressed sample, associated with the total pool of polysomes, whereas the protein of 22.95 kDa, which was present in the embryonic tissue of seeds germinating under unstressed conditions, disappeared. These changes may have affected both the stability and the translational capacity of polysomes.
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