Purification and properties of four monocot lectins from the family araceae (original) (raw)
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Vox Sanguinis, 1978
Extracts of seeds from 79 plant species were tested for agglutinating and lytic activity with the red cells of ten vertebrate species (man, monkey, rabbit, rat, goat, sheep, guinea pig, horse, fowl, dog). Of these extracts, 24 were hemagglutinating and 15 were hemolytic. The results suggest that some lectins can serve as useful diagnostic reagents in distinguishing the blood of one animal species from that of another.
Plant Lectins: Biochemical Characterization and Function
2013
The present paper is dedicated to plant lectins, their classifi cation, molecular structure, distribution in different plant organs and involvement in such biological functions as: cell to cell communication, phytoimmunity, symbiotic relationships, also cytotoxic action, mitogenic activity and participation in the immune reactions (system of complement). The future use of lectins in medical practice has been considered.
Bulgarian Journal of Agricultural Science, 2018
Zubčević, N., M. Fočak and D. Suljević, 2018. Highly specifi c hemagglutination activity of plant lectins in specifi c species: case of Fabaceae and Solanaceae. Bulg. J. Agric. Sci., 24 (3): 391–397 Lectins are carbohydrate-binding proteins present in most of the plants and in some animals. They possess the ability to agglutinate erythrocytes with known carbohydrate specifi city since they have at least one non-catalytic domain that binds reversibly specifi c monosaccharides or oligosaccharides. This study investigated the presence of lectins in the plant species of the family Fabaceae and Solanaceae. The results of our study have shown that 6 of 10 plant lectins caused agglutination, and 4 of them did not cause agglutination of human erythrocytes. Blood agglutination activity against A, B, AB and 0 groups was shown after exposing blood to lectin extracts obtained from 80% of tested plants in family Fabaceae, and 20% of tested plants in family Solanaceae. The highest degree of agglu...
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].
Identification and Characterization of Lectins from Leguminosae Plants
https://www.ijhsr.org/IJHSR\_Vol.9\_Issue.2\_Feb2019/IJHSR\_Abstract.017.html, 2019
Introduction: Since lectins are widely found in Leguminosae family due to their high protein content, in the present study, an attempt has been made to identify such legume lectins which have the agglutination properties with the red blood cells from normal individuals. Methods: Normal blood samples were collected, using the finger-prick technique. All blood samples were washed thrice in physiological saline and re-suspended at a concentration of 2% in normal saline. For ABO typing, standard serological procedure were followed. Results: In the results, various lectins showed the hemagglutination reaction pattern with human ABO blood groups. The lectin reacted with various blood groups with the strength of 1:1, 1:2, 1:4, 1:8, 1:16, 1:32, 1:64, and 1:128. Conclusion: The research findings were considered as the first step towards the field of sports nutrition. The lectin seeds are collected from the daily routine of the sports person, without knowing the effect of seeds on the body. Properly denaturized seeds should be consumed.
Agricultural and biological chemistry, 1990
Many plants have more than one lectin in a single organ or several organs. Some of them are producd by posttranslational modification, and others reflect multiple lectin genes in the plant. l) In winged bean (Psophocarpus tetragonolobus), two types of lectins so far, called acidic and basic lectins, have been purified from seeds. 2-5) Basic lectin has been purified from tubers too. 6) In a previous paper,7) we reported that one acidic lectin partially purified from green shells had hemagglutination properties similar to those of basic seed lectin. The accumulation of the knowledge on molecular and genetic aspects of plural lectins in plants is a help in revealing the unknown physiological role of plant lectins. l) In this connection, it is interesting which properties of this lectin are different