Lens culinaris lectin

E. Arce, P. M. Nieto, V. Diaz, R. Garcia Castro, A. Bemad, and J. Rojo, Glycodendritic structures based on Boltom hyperbranched polymers and their interactions with Lens culinaris lectin, Bioconjug. Chem., 14 (2003) 817-823. 

D-Glucose oxidase and peroxidase, when adsorbed on to concanavalin A-Sepharose or to Lens culinaris lectin-Sepharose have been used in an analytical system for the estimation of D-glucose. ... 

A membrane-associated glycoprotein has been solubilized by proteolytic digestion of membranes of rat mammary carcinoma cells. The material was not further characterized other than by its affinity for Lens culinaris lectin. A class of glycoproteins recognized as cell-surface markers by lectins and antibody appears to be expressed on the surface of embryonal carcinoma cells. Because of their unusual structural characteristics and abundance, the carbohydrate chains may play a role in the early stages of embryogenesis. 

A fluorimetric method for the thermodynamic and kinetic interpretation of lectin-receptor reactions has been validated in a study of the binding of rabbit erythrocytes to Lens culinaris lectin conjugated with fluorescein. It was demonstrated that under conditions when even a low number of receptors are saturated, most lectin molecules are univalently bound to the receptor. The high affinity for the membrane receptor, contrasting with the low affinity for specific monosaccharides, is explained by the very slow dissociation reaction which requires twice the energy of the association reaction. 

Kunitz bovine trypsin inhibitor Lens culinaris lectin... 

Lens culinaris lectin D-Mannan-protein copiplex... 

Hemagglutinating activity in the common lentil (Lens culinaris or Lens esculenta) was first reported by Landsteiner and Raubitschek.439 Several laboratories have since isolated the lentil lectin in pure form, and studied its physical-chemical properties and interaction with carbohydrates.138,142,143,440 442... 

A comparative study of the hemagglutinating activities of the pea (Pisum sativum), the lentil (Lens culinaris), and the jack-bean (Canavalia ensiformis) lectins towards the erythrocytes of fourteen different species showed446 that the pea and lentil lectins were, in all instances, more active than con A. Of great interest was the finding that, among these three lectins, con A alone was completely inactive against human erythrocytes (blood group, unspecified).446... 

Fig. 15.—Human IgA, Glycopeptide871 Showing the Carbohydrate-binding Loci for Various Lectins, [a. Limulus polyphemus b, Triticum vulgaris c, Ricinus communis d, Sophora japonica e, Abrus precatorius f, Cytisus sessilifolius g, Phaseolus vulgaris-, h, Canavalia ensiformis i, Lens culinaris j, Pisum sativus k, Vicia faba-, 1, Bandeiraea simplicifolia II m, Solanum tuberosum and n, Ulex europeus II.]...

For tumor-derived AFP, the composition of carbohydrate on AFP depends on the activity of saccharide transferase in the tumor cells. Differences in carbohydrate side chains on AFP may be determined by the binding of AFP to lectins, such as concanavahn A (Con A) and lens culinaris (LCA). Molecular variants of AFP can be separated into the liver type and the yolk sac type they differ from each other in their carbohydrate moiety. The yolk sac type of AFP contains... 

Like concanavalin A, the majority of lectins are associations of subunits. Sometimes they are identical, sometimes different, often numbering four, but sometimes more or less (two). Each of the two isolectins of lentils (lens culinaris. 

We measured recently the anisotropies of the Trp residues buried in the protein core of the lectin Lens culinaris agglutinin (LCA) and of those at its surface. We found that the protein core has restricted motions compared to the protein surface (the values of the anisotropies of the surface and of the buried Trp residues are 0.112 and 0.257, respectively) (Albani, 1996). 

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