Inhibition Reactions of Ten Nonspecific Seed Extracts and Their Conversion into Group Specific Lectins (original) (raw)
Related papers
Journal of The Chinese Chemical Society, 2004
Three lectins designated as CSL-1, CSL-2 and CSL-3 were purified from Cassia fistula seeds by gel filtration on Sephadex G-50 followed by ion-exchange chromatography on DEAE cellulose and finally by affinity chromatography on Sepharose 4B. The molecular weights of the lectins CSL-1, CSL-2 and CSL-3, determined by gel filtration on Sephadex G-75 column were 37,000, 42,400 and 46,000, and by SDS gel electrophoresis were 37500, 42000 and 46500, respectively. All three lectins agglutinated rat red blood cells and the agglutination was inhibited specifically by galactose and galactose containing saccharide. The neutral sugar contents of the lectins, CSL-1, CSL-2 and CSL-3 were estimated to be 3.5, 3.1 and 2.0%, respectively. The sugar composition of the lectins was found to be galactose in CSL-1, galactose and glucose in CSL-2, and galactose and mannose in CSL-3. The lectins exhibited maximum hemagglutinating activities around pH 7.2 to 7.5 and at a temperature range of 20°to 35°C. Biological activities of the lectins were abolished sequentially with the increase in concentration of acetic acid and denaturant solutions such as urea and guanidine-HCl.
Effect of plant lectins on human blood group antigens with special focus on plant foods and juices
Different plant lectins have been studied for lectin binding activity on ABO blood group system individ ually to study their suitability for consumption. 45% of plants were found to show blood group agglutination activity against A, B, AB and O groups. These results showed more suitability for consumption of investigated plants and their products to entire h uman population. Data also alarming human to be more careful about the plant lectins reacting with blood groups as th e similar reactions may possibly happen at mucosal surface of the gut . In fact, chemical composition on RBC may similar with mucosal cell surfaces of human gastrointestinal tract. In our investigation results reveal that 27 percent of plant extracts showed activity against A, 38 percent of plant extracts for B, 45 percent plant extracts on AB and 45 percent of plants on O group blood populat ions of human being s . Further, O blood group humans have shown more significant activity (10 different plants) than A, B and AB. Hence, these dou ble blind placebo studies are very promising and would give better results for suitability and digestibility of foods taking either as staple foods or juices, and also several health benefits for controlling the diet intake, based on the blood group type.
Screening and Partial Purification of Lectin from Various Bangladeshi Plant Seeds
American Journal of Sensor Technology, 2014
Lectins are group of proteins or glycoprotein of non immunological origins, which can recognize specific carbohydrate structure. In this research work hemaggulutination was used as technique for screening Bangladeshi vegetables for lectin. Five varieties of legume plant seeds Canavalia gladiata(Sword bean),Lens culinaris (Moshordal), Peasum sativam (Motorsuti), Vigna unguiculata subsp. sesquipedalis (Borboti), Cajanus cajan (Arhordal), one Amaranthaceae Amaranthus caudate (katoadata) and one fruit Citrullus lanatus (Watermelon) species from Bangladesh were examined for lectins with chicken and human erythrocytes. Crude extracts from all the species showed agglutinating activity against the erythrocytes used. The lowest protein concentration required to produce erythrocytes agglutination varied remarkable ranging from 0.7 µg/ml to 8080 µg/ml. The strongest activities were shown in the agglutination of human blood erythrocytes by partial purification of lectin from Moshordal and chick...
Purification and properties of a mitogenic lectin from Lathyrus sativus seeds
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
A mitogenic lectin has been isolated from saline extract of Lathyrus sativus by (NH4)2SO 4 precipitation, chromatography on DEAE-Sepharose and subsequent affinity chromatography on Sephadex G-100. The lectin has a molecular weight of 49000, as determined by ultracentrifugation, and consists of heavy (M r 19000) and light subunits (M r about 4400). The amino acid composition and N-terminal sequence of both subunits are given. The lectin agglutinated human erythrocytes of different ABO groups equally well, and the agglutination is inhibited best by D-mannose and D-glucose and their a-methyi-glucosides. High concentrations of the iectin were needed for optimal stimulation of human lymphocytes.
APPLICATIONS OF PLANT LECTINS IN BIOTECHNOLOGY AND THERAPEUTICS: Plant lectins application
The Journal of Microbiology, Biotechnology and Food Sciences, 2021
Lectins are carbohydrate-binding proteins broadly used in various therapeutic and biomedical applications. The variable affinity of lectins towards variety of carbohydrates has raised attention for the biologist to explore functional aspects of lectins. Lectins express specificity to simple carbohydrates for example mannose, lactose, sialic acid, complex glycan, and glycoproteins. Lectins are classified based on their sugar specificity and are used as a tool to study protein-carbohydrate interactions. Lectins are ubiquitous in nature and identified from all sources such as bacteria, fungi, algae, and animals. Plants are the most abundant source of lectins, and till now, more than three hundred lectins were characterized from plants. These are distributed to various parts of a plant according to their requirements and function. The physiological role of lectins in a plant is still not well understood. The overabundant presence of lectins in plant seeds and storage tissues indicated their role in plant development. Plant lectins shows a broad range of activities like antibacterial, antifungal, insecticidal, anticancerous, antileishmanial, antiviral, and anticoagulants. In this review, we aim to highlight the plant lectins classification and their application in various biological aspects. ARTICLE INFO
A new anti-H lectin from the seeds ofGalactia tenuiflora
Glycoconjugate Journal, 1986
A new anti-blood group H lectin was isolated from the seeds of Galactia tenuiflora. This lectin is mostly specific for the H type 2 trisaccharide but it shows some cross-reactivity with the H type 4 and H type 3 trisaccharides. Differences between this lectin and lectin 1 from Ulex europaeus are described. These differences concern the respective abilities of the lectins to recognize erythrocytes from some H deficient phenotypes, the inhibitions by salivas and the tissue distribution of the antigens recognized by the two lectins. The most important differences were noted in the surface epithelium of the stomach. This area is known to express ABH antigens under the control of the Se gene as defined by the Ulex europaeus lectin 1, yet it is always strongly labelled by the Galactia tenuiflora lectin irrespective of the secretor status of the tissue donor.
Biological Applications of Plants and Algae Lectins: An Overview
Carbohydrates - Comprehensive Studies on Glycobiology and Glycotechnology, 2012
Carbohydrates-Comprehensive Studies on Glycobiology and Glycotechnology 534 erythrocytes but not blood type B or O cells, whereas the extract of Lotus tetragonolobus agglutinated only blood type O erythrocytes [1,5]. The specific interaction between lectins and carbohydrates of erythrocytes played a crucial role in the investigations of the antigens associated with the ABO blood group system. In the subsequent decade, Morgan and Watkins found that the agglutination of type A erythrocytes by extracts of Phaseolus limensis was best inhibited by α-linked N-acetyl-Dgalactosamine, while the agglutination of O cells by the extract of L. tetragonolobus was best inhibited by α-linked L-fucose [6]. Around thirty years after Boyd, the research on lectins reached the molecular level studies. It was clear the need to a better understanding on the structural aspects of lectins. Then, in 1972 Edelman and colleagues established the primary sequence of ConA [6]. In the same year, Edelman's group and independently Karl Hardman with Clinton Ainsworth, solved the 3D structure of ConA by X-ray crystallography [7,8]. 2. What exactly is a lectin? In 1954 Boyd and Shapleigh proposed the term lectin, from the Latin verb legere (which means "to select"). This term was based on the fact that these proteins have the ability to distinguish between erythrocytes of different blood types [9]. Lectins were early defined as carbohydrate-binding proteins of nonimmune origin that agglutinate cells or as carbohydrate-binding proteins other than antibodies or enzymes. However, these definitions were updated, since some plant enzymes are fusion proteins composed of a carbohydrate-binding and a catalytic domain, for instance, type 2 RIPs, such as ricin and abrin, are fusion products of a catalytically active A-chain (which has the Nglycosidase activity) and a carbohydrate-binding B-chain, both linked by a disulfide bond [10]. Furthermore, there is in nature carbohydrate-binding proteins possessing only one binding site and, therefore, are not capable of precipitating glycoconjugates or agglutinating cells [11]. Thus, in 1995 Peumans and Van Damme proposed the most suitable definition for lectins. According to the "new" definition, all plant proteins that possess at least one noncatalytic domain that binds reversibly to a specific mono-or oligosaccharide are considered as lectins [12,13]. 2.1. Plant lectins Lectins are proteins widely distributed in nature such in microorganisms, plants, animals and humans, acting as mediators of a wide range of biological events that involve the crucial step of protein-carbohydrate recognition, such as cell communication, host defense, fertilization, cell development, parasitic infection, tumor metastasis, inflammation, etc [14-15]. Peumans and Van Damme classified the plant lectins according to their overall structure. Merolectins consist exclusively of a single carbohydrate-binding domain (e.g. hevein, a Biological Applications of Plants and Algae Lectins: An Overview 535 chitin-binding latex protein isolated from the rubber tree Hevea brasiliensis). Since merolectins have a unique carbohydrate-binding site, they are incapable of precipitating glycoconjugates or agglutinating cells. Hololectins are also built of carbohydrate-binding domains. However, they contain at least two such domains that are identical or very similar. Because these lectins are di-or multivalent they can agglutinate cells and/or precipitate glycoconjugates. Most plant lectins are hololectins. Superlectins are built of at least two carbohydrate-binding domains. Unlike hololectins, these domains are not identical or similar. Thus, superlectins recognize structurally different sugar (e.g. TxLCI, a tulip bulb lectin that recognizes mannose and N-acetyl-galactosamine). Chimerolectins are fusion proteins that consist of two different chains, one of them with a remarkable catalytic activity (or another biological activity). RIPs type 2 are examples of chimerolectins [11-12].
Purification and properties of four monocot lectins from the family araceae
Phytochemistry, 1995
Four new monocot lectins from the tubers of araceous plants, namely, Arisaema consanguineum Schott (ACA), A. curvature Kunth (ACmA) and Sauromatum guttatum Schott (SGA) from the tribe Areae, and Gonatanthus pumilus D. Don (GPA) from the tribe Colocasieae have been purified by affinity chromatography on asialofetuinlinked amino activated silica beads. These lectins possess similar physicochemical and biological properties. All the lectins gave a single peak on HPLC size exclusion and cation exchange columns, and a single band on PAGE, (pH 4.5). In SDS-PAGE, all the lectins gave a single band corresponding to a subunit of Mr 13 000. All the lectins yielded multiple peaks on anion-exchange column, multiple bands on non-denatured PAGE (pH 8.3) and a family of bands on isoelectric focusing. The lectins agglutinate rabbit, rat and sheep red blood cells (RBCs) but are inactive towards human ABO erythrocytes. The haemagglutination activity of these lectins is inhibited by asialofetuin only, while simple sugars/derivatives including chitin, porcine mucin and fetuin did not react. In serological studies against rabbit anti-SGA serum, all four lectins produced immunoprecipitin lines. The lectins within each tribe were identical but the lectins belonging to the tribe Areae were only partially identical to the lectins from the tribe Colocasieae.
International Journal of Biological Macromolecules, 2008
The N-acetyl-galactosamine specific lectin from Macrotyloma axillare seeds (LMA) was purified by precipitation and ion exchange chromatography. The LMA 0.2 mol L −1 fraction showed hemagglutinating activity on erythrocytes A1. The results for molecular mass determinations were about 28 kDa. The LMA pHdependent assays showed best hemagglutinating activity at pH 6.0-8.0; being decreased at acidic/alkaline conditions and by EDTA treatment. LMA is a tetramer at pH 8.2 and a dimer at pH 4.0. Human erythrocytes from ABO system confirmed the A1 specificity for LMA. This new methodology is useful and easy, with low costs, for lectin purification in large amounts.