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|Lycopersicon esculentum : Tomato|
LEA, TL, LEL
Molecular structure of
Tomato:LEA, TL, LEL
|Lecster ID:418|| Edit Entry |
| Common Nomenclature:||LEA, TL, LEL|
|Characterization Notes:||For differential binding patterns in endothelial tissue, see: Eur J Cell Biol 1990 Feb;51(1):85-95 For discussion of immunosupressive nature of tomato lectin and its possible clinical relevance, see: Lect. Biol. Biochem. Clin. Biochem. 1985 (4); 3 Tomato lectin has been used for the isolation of glycoproteins and the controlled oral delivery of drugs. See : Pharm. R. 1992 (9); 547-553 LEA is serolgically related to (though not identical with) the lectins from the Solanaceae species Solanum tuberosum (potato) and Datura stramonium (thornapple). See: FEBS Letters 1980 (113);128-133|
|Biological Activity:||Tomato lectin is a very stable glycoprotein containing about 50 percent arabinose and galactose. This lectin is composed of a single polypeptide of about 100,000 daltons that may form aggregates in solution. Like other lectins that bind N-acetylglucosamine oligomers, tomato lectin prefers trimers and tetramers of this sugar. Tomato lectin, although sharing some specificities with potato, Datura lectin and wheat germ agglutinin, has been reported to be dissimilar in many respects. Tomato lectin binds well to such glycoproteins as glycophorin and Tamm-Horsfall glycoprotein.|
Tomato lectin (from Lycopersicon esculentum) is an effective marker of blood vessels and microglial cells in rodents. Conjugation of the lectin with a fluorophore facilitates fast, one-step detection and visualization using intravascular perfusion methods or direct application to tissue sections.
LEA agglutinates human and animal erythrocytes. LEA is non-mitogenic for mouse and chicken lymphocytes but it dose-dependently inhibits the mitogenic effects of ConA, PHA and Pokeweed Mitogen in chickens. See: J Biol Chem 1980 Mar 10;255(5):2056-61
See also: Tomato Lectin in Brain Research
|Source Tissue:||LEAoccurs in all tissues of the tomato, but is located predominantly in the locular fluid of ripe fruits. See: Biochem J. 1980 (185); 269-272|
|Inhibitors:||Hemagglutination inhibition studies show that the binding site is most complemetary to three (or possibly four) ß-(1,4) linked GlcNAc units. See: J Biol Chem 1980 Mar 10;255(5):2056-61|
|References:||J Biol Chem 1980 Mar 10;255(5):2056-61|
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