Interaction of Glucose/Sucrose Binding Lectin Isolated from Nigeria Wild Bean with E. coli and S. aureus</i> (original) (raw)
Related papers
There were performed in vitro interactions of five plant lectins purified by affinity chromatography with seven pathogenic bacteria cultivated in liquid media. The positive results were scored by the degree of bacterial cells agglutination. There have been noticed strong agglutinations of Salmonella typhymurium and Salmonella gallinarum with the lectins isolated from pumpkin seeds, potato buds and potato tubers. Escherichia coli and Pseudomonas aeruginosa were better agglutinated by vegetable marrow and pumpkin seeds lectins and weaker by potato buds and tubers lectins. Glutaraldehyde immobilization of the lectin isolated from potato buds resulted in an insoluble polymer suspension. The interaction of the lectin polymer suspension with the liquid cultures of Salmonella and Pseudomonas was quantified by measuring the OD (660 nm) at time 0 and after 10 minutes of standing. The decrease of the OD demonstrated that immobilized insoluble lectin polymer bound bacterial cells and the aggre...
International Journal of Advanced Academic Research, 2016
Lectins was extracted from processed and unprocessed black-eyed peas, green beans, soybeans, peanuts, and red kidney beans by grinding using attrition mill and then soaked in distilled water. The proteins in the supernatant were precipitated by dissolving 10g of ammonium sulphate in 100ml of the supernatants. The lectin extracts were evaluated for hemagglutinin activity using human erythrocytes from blood group A + , B + , AB + , and O + , respectively. Result revealed that lectins from unprocessed soybean, black-eyed pea and green bean are blood group selective and may be classified as blood type specific lectins. While lectins from kidney beans and peanuts agglutinated all blood groups and may be classified as panhemagglutinin lectins, i.e. they agglutinated erythrocytes from all blood groups. Result shows that blood group O is less affected by hemagglutinin activity of lectin. Reduction/loss of hemagglutinin activity was observed with reduction in concentration of the crude lectin extracts in all unprocessed legumes. Boiling (at 100 0 C) for 30minutes completely inactivated hemagglutinin activity of lectin in Black eyed peas, soybeans, green beans and red kidney beans. Slight hemagglutinin activity was seen in lectin from roasted peanuts, indicating that dry heating may be very effective method to inactivate lectin completely. Also, in this study, lectins were extracted from rice (Oryza sativa), maize (Zea mays), sorghum (Sorghum bicolor), Acha (Digitaria excells), millet (Panicum maniceum); partial purification of the extract assayed from hemugglutinin activity using 4% of human erythrocyte in lectin buffer. Extract from these selected cereals showed positive and negative agglutination reaction with blood group A + , B + , O + and AB + depending on the concentration (dilution) and the blood group. Lectin extract from maize showed no agglutination reaction when diluted in blood group A + , B + , and AB + and even when processed and diluted. While crude lectin extract from rice showed no activity in blood group A + , B + , and AB + and when unprocessed and showed lectin agglutination activity when processed by boiling (cooking) showing that heat may encourage its activity. Blood group B + , and AB + showed no activity in all dilution. Also acha showed high agglutination activity in blood group A + , B + , AB + and O + but losses activity in dilution a 2 and a 3. Crude lectin extract from processed sorghum showed
Journal of Food Processing and Preservation, 1991
The effects of several processing methods on the hemagglutinating activity of ten varieties of dry beans (Phaseolus vulgaris L.) were studied using a serial dilution technique. Lectin activity ranged from 128-512 X 10" unitslg whole bean flour, with a mean value of 307 x 104 unitslg bean. Small Red and Kidney bean types had the highest agglutinating activities among the varieties studied. N o noticeable changes were observed upon dehulling beans, while germinated beans and protein concentrates had lower hemagglutinating activity. Cooking of beans completely destroyed the lectin activity.
International Journal of Research and Analytical Reviews (IJRAR) , 2024
A protein fraction exhibiting lectin activity was identified in the extract of local Roman bean (Phaseolus vulgaris) sprouts. The galactose-specific lectins demonstrated the highest activity. The galactose-specific lectin (BS-Gal) was purified using affinity chromatography on an ES-2100-100 column. Gel electrophoresis revealed that BS-Gal consists of two protein subunits with molecular weights of 60 and 54 kDa, respectively. Various physicochemical properties of the lectin were investigated, showing optimal activity within a pH range of 7-9 and temperatures from 0 to 75 °C, beyond which its hemagglutinating activity diminishes. The lectin displayed high sensitivity to divalent ions and certain amino acids. Calcium and magnesium ions significantly contribute to the structural integrity of the lectin, as indicated by changes in hemagglutinating activity in the presence of EDTA and EGTA. Additionally, BS-Gal was found to bind to human erythrocytes expressing A and B antigens.
Hemagglutinin Activities of Lectin Extracts from Selected Legumes
Researchgate, 2020
The legumes-Mucuna, Cowpea, Pigeon pea, African Yam Bean, Black-eyed pea, Soybean, Red kidney bean, Peanut, Green bean, and Bambara-were obtained from markets in Umuahia, ground in flour using Art's Way Roller Mill. Crude lectins were extracted from the milled legumes by soaking in distilled water for over 12 hours, followed by decanting; the proteins in the supernatant were precipitated by dissolving 10g of ammonium sulfate in 100ml of the supernatants. The crude lectin extracts were evaluated for hemagglutinin activity, using human erythrocytes. Mucuna lectins were specific for blood groups B + and AB +. Cowpea lectins agglutinated group A + and B +. African yam bean and Bambara lectins agglutinated all, while Pigeon pea was specific for groups A + , B + and O +. Mucuna cowpea, Pigeon pea, lectin was blood specific, while African yam bean and Bambara lectins were not. Lectins from Soybean, Black-eyed pea, and Green bean were blood group selective; while lectins from Kidney beans and Peanuts were pan-hemagglutinin lectins. Blood group O was less affected. Reduction in hemagglutinin activity was observed with a reduction in the concentration of the crude lectin extracts.
Purification and Characterization of a Lectin fromPhaseolus vulgaris cv.(Anasazi Beans)
Journal of Biomedicine and Biotechnology, 2009
A lectin has been isolated from seeds of thePhaseolus vulgaris cv.“Anasazi beans” using a procedure that involved affinity chromatography on Affi-gel blue gel, fast protein liquid chromatography (FPLC)-ion exchange chromatography on Mono S, and FPLC-gel filtration on Superdex 200. The lectin was comprised of two 30-kDa subunits with substantial N-terminal sequence similarity to otherPhaseoluslectins. The hemagglutinating activity of the lectin was stable within the pH range of 1–14 and the temperature range of 0–80∘C. The lectin potently suppressed proliferation of MCF-7 (breast cancer) cells with anIC50of 1.3 μM, and inhibited the activity of HIV-1 reverse transcriptase with anIC50of 7.6 μM. The lectin evoked a mitogenic response from murine splenocytes as evidenced by an increase in [3H-methyl]-thymidine incorporation. The lectin had no antifungal activity. It did not stimulate nitric oxide production by murine peritoneal macrophages. Chemical modification results indicated that t...
International Journal of Research in Ayurveda & Pharmacy, 2013
Lectin from Erythrophleum suaveolens stem bark was partially purified and evaluated in terms of its haemagglutination activity. Ground, dried stem bark of Erythrophleum suaveolens was extracted by aqueous method and the protein extract was concentrated in 20-90 % saturation. The ammonium sulfate precipitate was subjected to gel filtration chromatography using Sephadex G-75 resin and fractions were tested for haemagglutination activity. The two fractions obtained with the highest hemmaglutinating activity were further subjected separately to ion-exchange chromatography using Sp-Sephadex C-50 resin. Isolated lectins were found to agglutinate chicken erythrocytes; fractions from gel filtration chromatography showed haemagglutinating activity of 0.1 HU/µL and 0.091 HU/µL, while the ion exchange fractions showed haemagglutinating activity of 0.05 HU/µL and all were stable at the temperature range of 30-60 0 C and pH range of 3-7. The carbohydrate content of the crude extract, Gel I, Gel II, Ion I and Ion II fractions were 0.04 %, 0.04 %, 0.03 %, 0.02 %, respectively. The crude and purified lectins inhibited agglutination in the presence of mannose and Nacetyl-glucoseamine sugars and showed five bands at positions 38kDa, 28kDa, 26kDa, 11kDa and 9kDa on a SDS-PAGE electrophoregram.
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...
Hydrophobic binding properties of the lectin from lima beans (Phaseolus lunatus)
Journal of Biological Chemistry, 1982
Hydrophobic binding to the lectin from lima beans (Phaseolus lunatus) was studied by lectin-induced alterations in the fluorescence and absorption spectra of several hydrophobic ligands. The fluorescence of 1,8-anilinonaphthalenesulfonic acid (ANS) was greatly enhanced in the presence of lima bean lectin with concomitant shift of the fluorescence emission maximum from 520 to 469 nm. Similar enhancement was seen with 2,6-toluidinylnaphthalenesulfonic acid (TNS) with a shift of emission from 500 to 423 nm, and with an uncharged analogue, N-phenyl-1-naphthylamine. Fluorescence titrations with ANS and rose bengal yielded affinity constants of 3.9 X 10(3) and 6 X 10(5) M-1, respectively. Fluorescence titration with TNS indicated binding heterogeneity and yielded intrinsic association constants of 7.8 X 10(4) and 2.2 X 10(3) M-1 assuming a model with two classes of independent sites. The high affinity binding had an apparent stoichiometry of 1.08 sites/lectin tetramer. Equilibrium dialysis for ANS and TNS confirmed the results of fluorescence titration and gave stoichiometries for ANS and low affinity TNS binding of one site/subunit. Neither chemical modification of thiol groups known to be essential for carbohydrate binding nor titration in the presence of haptenic sugar affected the binding of ANS or TNS to the lectin. These results indicated that the carbohydrate and hydrophobic binding sites of lima bean lectin are independent and noninteracting.
Lectin-like activity of Lactobacillus acidophilus strain JCM 1026
FEMS Microbiology Letters, 1992
The lectin-like activity of the Lactobacillus acidophilus strain JCM 1026 was studied by hemagglutination and hemagglutination-inhibition assays. L. acidophilus strain JCM 1026 was found to hemagglutinate human and animal erythrocytes. Neuraminidase-treatment of human-type O erythrocytes enhanced the activity. Treatment of the bacterial cells with proteinase K reduced hemagglutinating activity significantly. Although several mono- and disaccharides did not inhibit hemagglutination, several different glycoproteins did. These data indicate that a proteinaceous lectin-like component(s) recognizing carbohydrate-containing molecules is located on the cell surface of L. acidophilus.