Seed lectin

Lectins (proteins and/or glycoproteins of non-immune origin that agglutinate cells, from seeds of Robinia pseudoacacia), M 100,000. Purified by pptn with ammonium sulfate and dialysis then chromatographed on DE-52 DEAE-cellulose anion-exchanger, hydroxylapatite and Sephacryl S-200. [Wantyghem et al. Biochem J 237 483 1986.]... 

SPARVOLIF, GALLO A, MARiNELLi D, SANTUCCi A, BOLLiNi R (1998) Novel lectin-related proteins are major components in lima bean Phaseolus lunatus L.) seeds. Biochim Biophys Acta. 1382 311-23. 

Several carbohydrate-binding proteins have been isolated from Sambucus nigra and two haemagglutinins have been isolated from its bark. Its seeds contain a lectin that is related to the immunological properties of the bark. One of its carbohydrate-binding proteins, called nigrin, is made of two subunits and is reported to cause red blood cells to clump. 5... 

J. J. Calvete, C. F. Santos, K. Mann, T. B. Grangeiro, M. Nimtnz, C. Urbanke, and B. S. Cavada, Amino acid sequence, glycan structure, and proteolytic processing of the lectin of Vatairea macrocarpa seeds, FEBS Lett., 452 (1998) 286-292. 

Lectin affinity chromatography may be used to purify a range of glycoproteins. Lectins are a group of proteins synthesized by plants, vertebrates and a number of invertebrate species. Especially high levels of lectins are produced by a variety of plant seeds. Plant lectins are often termed... 

It was noted, however, that legume seeds contain anti nutritional factors such as trypsin inhibitors and lectins which exert... 

Other approaches to induce gastrointestinal discomfort have far more serious toxic effects. The chemical colchicine stops cell division (an antimitotic), producing severe nausea, vomiting, and dehydration, which can lead to delirium, neuropathy, and kidney failure. On the other hand, colchicine is used in the treatment of gout and has been studied as an anticancer agent because it stops cell division. Most toxic of all are plants that produce lectins, and the most toxic of these is the chemical ricin produced by castor beans. Only 5 to 6 seeds are necessary to kill a small child. Fortunately, following oral consumption much of the ricin is destroyed in the stomach. Ricin is extremely effective at stopping protein synthesis, so much so that direct exposure to only 0.1 pg/kg can be fatal. 

N.A. Ricinoleic acid, ricin, ricinine, lectins.99 The seeds are toxic. Laxative, prompting a bowel movement. 

In this Section will be discussed plant lectins that specifically bind to a-D-galactopyranosyl residues. Lectins of a special class that are specific for j8-D-glycosidic linkages487 also exist in the seeds and other tissues of plants. Various aspects of lectins have been reviewed by Goldstein and Hayes.488... 

Plant lectins (also termed agglutinins, hemagglutinins, and phytohemagglutinins) are glycoprotein macromolecules that are capable of specific, noncovalent binding to carbohydrates.489 Lectins are known to occur widely in the seeds of plants488 however, they have also been... 

Relative Affinities of Some Seed-lectins for o-D-Galsctopyranosyl Residues44 ... 

Kabir, S. (1998) Jacalin a jackfruit (Artocarpus heterophyllus) seed-derived lectin of versatile applications in immunobiological research. J. Immunol. Methods 212, 193-211. 

Faba beans contain several ANFs such as tannins, protease inhibitors (vicin/ convicin) and lectins. Use of low-vicin/convicin cultivars may allow substantial levels of faba beans to be included in poultry diets (Danner, 2003). The levels of trypsin inhibitor and lectin activities are low compared with other legume seeds and do not pose problems in poultry diets when faba beans are incorporated into diets at the levels shown below. Of most concern for poultry is the tannin fraction, which has been shown to depress digestibility of the protein and AA (Ortiz et al., 1993). Tannins in whole faba beans are associated with the seedcoat (testa), and the tannin content is related to the colour of the seedcoat (and flowers). Tannins are lower in white than in the colour-seeded varieties. 

In common with many other legume seeds, raw lentils contain some undesirable constituents, although the levels of these are not likely to be of concern in poultry feeding. Weder (1981) reported the presence of several protease inhibitors in lentils. Marquardt and Bell (1988) also identified lectins (hemagglutinins), phytic acid, saponins and tannins as potential problems but could find no evidence that these had adversely affected performance of pigs fed lentils. It is known that cooking improves the nutritive value of lentils for humans but the effects of consumption of raw lentils by non-ruminants have not been well documented (Castell, 1990). 

TAIPALENSUU, J., ERIKSSON, S., RASK, L., The myrosinase-binding protein from Brassica napus seeds possesses lectin activity and has a highly similar vegetatively expressed counterpart., Eur. J. Biochem., 1997,250,680-688. 

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