Myanamr Health Research Registration 2021; 33(1): 37-43.
Effects of Euphorbia tortilis (Shar-zaung) Latex Lectin on Human Erythrocyte Agglutination
Myanmar Health Sciences Research JournalABSTRACT
Lectin containing plants have been found in many botanical groups including mono and dicotyledons, molds and lichens. The lectins can be detected mostly in seeds, but they can also be found in other vegetative parts of the plants such as roots, leaves, barks, rhizomes, bulbs and plant exudates. Latex is a milky sap containing proteins, carbohydrates, lipids, amino acids, vitamins, several enzymes and other essential inorganic salts.
Lectins are a group of carbohydrate-binding proteins of non-immune origin, capable of specific recognition of and reversible binding to carbohydrate moieties of complex glyco-conjugate without chemically modifying them. They agglutinate cells and/or precipitate glycoconjugates. Lectins can be found in animals, plants, and microorganisms. Plant lectins are regarded as carbohydrate-binding proteins although differing in their molecular structures, carbohydrate-binding specificities and biochemical activities. Some may bind mannose-containing oligosaccharides while others bind galactose-containing structures.1
Euphorbia tortilis latex was collected from the plant growing in experimental garden of School of Life Sciences of University of Hyderabad, India.
Protein molecular mass standards for SDS-PAGE (phosphorylase b, 97.4 kDa; bovine serum albumin, 68 kDa; ovalbumin, 43 kDa; carbonic anhydrase, 29 kDa; soyabean trypsin inhibitor, 20 kDa; lysozyme, 14.3 kDa) were purchased from Genei, Bangalore, India. Divinylsulfone and sepharose-6B were purchased from Sigma Chemical Company, USA. All other chemicals/reagents used were of analytical grade manufactured from India by different firms.
The studies of lectins, which have been isolated from the latex of some Euphor-biaceae species, suggested that plant lattices are rich source of lectins. Until now, lectins from latex have been reported from six genera, i.e. Euphorbia, Hevea, Hura, Mona-denium, Pedilanthus and Synadenium. Except Hevea lectin, all are galactose-specific. In this study, a galactose-specific lectin (ETLA) was isolated from the latex of Euphorbia tortilis (Spiral cactus). The method used to purify this lectin by affinity chromatography on sepharose 6B column was simple and very efficient, yielding about 1.92 mg/ml of purified lectin protein
The author declares that there is no competing interest.