Precipitation Reactions Between Components of Plant Tissue Extracts

1975 ◽  
Vol 2 (4) ◽  
pp. 533 ◽  
Author(s):  
MA Jermyn
Keyword(s):  
Concanavalin A ◽  
Carbohydrate Binding ◽  
Exact Nature ◽  
Plant Seeds ◽  
Tissue Extracts ◽  
General Inhibitor ◽  
Precipitation Reactions ◽  
Leguminous Seeds ◽  
Gel Diffusion ◽  
Seed Extracts

Precipitation lines are observed on gel-diffusion plates between many pairs of seed extracts. Interactions involving Canavalia ensiformis depend upon concanavalin A, and a number of extracts from other plant seeds contain a precipitant that mimics that lectin. Methyl a-D-mannopyranoside is a general inhibitor of the precipitation phenomenon and some form of protein-carbohydrate binding seems to be involved in all precipitations, although the exact nature of the macromolecules taking part is obscure. For the leguminous seeds Phaseolus vulgauis, Vicia faba and Cajanus cajan, precipitation reactions occur between extracts of cotyledons and extracts of tissues of the parent plants, even of the testa of the seeds. The nature of these reactions appears to be the same as those of the interspecies ones. Both types of reaction may be examples of ways in which plant cells recognize self from non-self. The material in P. vulgaris that reacts with concanavalin A is a group of globulin-like glycoproteins (5 % carbohydrate), heterogeneous in both charge and molecular weight but similar in overall amino acid analysis.

Leguminous Seed Glycoproteins That Interact With Concanavalin A

1977 ◽  
Vol 4 (1) ◽  
pp. 25 ◽  
Author(s):  
PA Gleeson ◽  
MA Jermyn
Keyword(s):  
Concanavalin A ◽  
Coffea Arabica ◽  
Sodium Dodecyl ◽  
Con A ◽  
Precipitation Line ◽  
Leguminous Seed ◽  
Protein Staining ◽  
Gel Diffusion ◽  
Haemagglutination Activity ◽  
Seed Extracts

Material that interacts with concanavalin A has been purified from seed extracts of 18 species (16 legumes, Coffea arabica and Lolium perenne) by Con A-Sepharose chromatography. When examined by sodium dodecyl sulphate-polyacrylamide disc gel electrophoresis, many of the preparations showed a number of protein-staining components. All the preparations gave a single precipitation line against Cunalialia ensiformis crude extract on gel diffusion plates. Some of the con A-interacting preparations were shown to possess haemagglutination activity. The Arachis hypogaea (peanut) preparation contains one major glycoprotein of molecular weight 69 000, which was further purified and analysed. The purified glycoprotein contains 12% carbohydrate, galactose being the major sugar with minor amounts of mannose and xylose present.

scholarly journals Lectin and E. coli Binding to Carbohydrate-Functionalized Oligo(ethylene glycol)-Based Microgels: Effect of Elastic Modulus, Crosslinker and Carbohydrate Density

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 263
Author(s):  
Fabian Schröer ◽  
Tanja J. Paul ◽  
Dimitri Wilms ◽  
Torben H. Saatkamp ◽  
Nicholas Jäck ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Elastic Modulus ◽  
Ethylene Glycol ◽  
Concanavalin A ◽  
Specific Binding ◽  
Network Density ◽  
Carbohydrate Binding ◽  
E Coli ◽  
Surface Recognition ◽  
Strong Anchoring

The synthesis of carbohydrate-functionalized biocompatible poly(oligo(ethylene glycol) methacrylate microgels and the analysis of the specific binding to concanavalin A (ConA) and Escherichia coli (E. coli) is shown. By using different crosslinkers, the microgels’ size, density and elastic modulus were varied. Given similar mannose (Man) functionalization degrees, the softer microgels show increased ConA uptake, possibly due to increased ConA diffusion in the less dense microgel network. Furthermore, although the microgels did not form clusters with E. coli in solution, surfaces coated with mannose-functionalized microgels are shown to bind the bacteria whereas galactose (Gal) and unfunctionalized microgels show no binding. While ConA binding depends on the overall microgels’ density and Man functionalization degree, E. coli binding to microgels’ surfaces appears to be largely unresponsive to changes of these parameters, indicating a rather promiscuous surface recognition and sufficiently strong anchoring to few surface-exposed Man units. Overall, these results indicate that carbohydrate-functionalized biocompatible oligo(ethylene glycol)-based microgels are able to immobilize carbohydrate binding pathogens specifically and that the binding of free lectins can be controlled by the network density.

scholarly journals Effects of some indigenous plant seed extracts on the Haematology of a predatory fish Singhi Heteropneustes fossilis (Bloch)

2013 ◽  
Vol 6 (1-2) ◽  
pp. 11-25
Author(s):  
Munira Nasiruddin ◽  
Mohammad Ali Azadi ◽  
Monika Rahman ◽  
Israt Ara Shazia Rahman
Keyword(s):  
Blood Parameters ◽  
Acacia Auriculiformis ◽  
Predatory Fish ◽  
Heteropneustes Fossilis ◽  
Plant Seed ◽  
Alcohol Extract ◽  
Plant Seeds ◽  
Indigenous Plant ◽  
Clerodendrum Viscosum ◽  
Seed Extracts

Haemolytic effects of different extracts of five indigenous plant seeds viz. Datura innoxia (Mill) (Shada Dhutra), Clerodendrum viscosum (Vent.) (Vat), Amoora rohituka (Roxb.) Wt. ct. Arnott (Pitraj), Acacia auriculiformis A. Cunn. Ex. Benth. (Akashmoni) and Pongamia pinnata (L.) Pierre (Karinja) were studied upon a predatory fish, Singhi, Heteropneustes fossilis (Bloch) under laboratory conditions. Toxicants inducing effects on the blood parameters included decreased RBC and WBC counts, low haemoglobin percentage and decreased PCV (packed cell volume), MCV (mean corpuscular volume) and MCH (mean corpuscular haemoglobin). Haemolysis action included shrunken or swollen RBCs, granulated nuclei of RBCs and pyknotic nuclei of WBCs, clumping of RBCs and syncitium of RBC matrix. Damage of blood cells with absolute ethyl alcohol extract was most pronounced with all of the seed extracts. The order of toxicity of the five seed extracts on the blood parameters of Singhi was: D. innoxia < A. auriculaerformis < P. pinnata < C. viscosum < A. rohituka seed extracts. On the basis of haemolysis the toxicity was: A. rohituka > C. viscosum > P. pinnata > D. innoxia > A. auriculiformis seed extracts. DOI: http://dx.doi.org/10.3329/cujbs.v6i1-2.17078 The Chittagong Univ. J. B. Sci.,Vol. 6(1&2):11-25, 2011

Immunoreactivity for canatoxin and concanavalin A among proteins of leguminous seeds☆

1988 ◽  
Vol 27 (1) ◽  
pp. 25-30 ◽  
Author(s):  
Celia R. Carlini ◽  
Grace B.S. Barcellos ◽  
Arthur D.V. Baeta-neves ◽  
Jorge A. Guimarães
Keyword(s):  
Concanavalin A ◽  
Leguminous Seeds

scholarly journals Effects of some indigenous plant seed extracts on the haematology of a predatory fish singhi Heteropneustes fossilis (Bloch)

2013 ◽  
pp. 27-36
Author(s):  
Munira Nasiruddin ◽  
Mohammad Ali Azadi ◽  
Monika Rahman ◽  
Israt Ara Shazia Rahman
Keyword(s):  
Blood Parameters ◽  
Acacia Auriculiformis ◽  
Predatory Fish ◽  
Heteropneustes Fossilis ◽  
Plant Seed ◽  
Alcohol Extract ◽  
Plant Seeds ◽  
Indigenous Plant ◽  
Clerodendrum Viscosum ◽  
Seed Extracts

Haemolytic effects of different extracts of five indigenous plant seeds viz. Datura innoxia (Mill) (Shada Dhutra), Clerodendrum viscosum (Vent.) (Vat), Amoora rohituka (Roxb.) Wt. ct. Arnott (Pitraj), Acacia auriculiformis A. Cunn. Ex. Benth. (Akashmoni) and Pongamia pinnata (L.) Pierre (Karinja) were studied upon a predatory fish, Singhi, Heteropneustes fossilis (Bloch) under laboratory conditions. Toxicants inducing effects on the blood parameters included decreased RBC and WBC counts, low haemoglobin percentage and decreased PCV (packed cell volume), MCV (mean corpuscular volume) and MCH (mean corpuscular haemoglobin). Haemolysis action included shrunken or swollen RBCs, granulated nuclei of RBCs and pyknotic nuclei of WBCs, clumping of RBCs and syncitium of RBC matrix. Damage of blood cells with absolute ethyl alcohol extract was most pronounced with all of the seed extracts. The order of toxicity of the five seed extracts on the blood parameters of Singhi was: D. innoxia < A. auriculiformis < P. pinnata < C. viscosum < A. rohituka seed extracts. On the basis of haemolysis the toxicity was: A. rohituka > C. viscosum > P. pinnata > D. innoxia > A. auriculiformis seed extracts. DOI: http://dx.doi.org/10.3329/cujbs.v5i1.13367 The Chittagong Univ. J. B. Sci.,Vol. 5(1 &2):27-36, 2010

scholarly journals Redistribution and shedding of flagellar membrane glycoproteins visualized using an anti-carbohydrate monoclonal antibody and concanavalin A.

1986 ◽  
Vol 102 (5) ◽  
pp. 1797-1812 ◽  
Author(s):  
R A Bloodgood ◽  
M P Woodward ◽  
N L Salomonsky
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
High Molecular Weight ◽  
Concanavalin A ◽  
Live Cells ◽  
Surface Phenomenon ◽  
Carbohydrate Binding ◽  
Membrane Glycoproteins ◽  
Western Blots ◽  
Flagellar Membrane

Two carbohydrate-binding probes, the lectin concanavalin A and an anti-carbohydrate monoclonal antibody designated FMG-1, have been used to study the distribution of their respective epitopes on the surface of Chlamydomonas reinhardtii, strain pf-18. Both of these ligands bind uniformly to the external surface of the flagellar membrane and the general cell body plasma membrane, although the labeling is more intense on the flagellar membrane. In addition, both ligands cross-react with cell wall glycoproteins. With respect to the flagellar membrane, both concanavalin A and the FMG-1 monoclonal antibody bind preferentially to the principal high molecular weight glycoproteins migrating with an apparent molecular weight of 350,000 although there is, in addition, cross-reactivity with a number of minor glycoproteins. Western blots of V-8 protease digests of the high molecular weight flagellar glycoproteins indicate that the epitopes recognized by the lectin and the antibody are both repeated multiple times within the glycoproteins and occur together, although the lectin and the antibody do not compete for the same binding sites. Incubation of live cells with the monoclonal antibody or lectin at 4 degrees C results in a uniform labeling of the flagellar surface; upon warming of the cells, these ligands are redistributed along the flagellar surface in a characteristic manner. All of the flagellar surface-bound antibody or lectin collects into a single aggregate at the tip of each flagellum; this aggregate subsequently migrates to the base of the flagellum, where it is shed into the medium. The rate of redistribution is temperature dependent and the glycoproteins recognized by these ligands co-redistribute with the lectin or monoclonal antibody. This dynamic flagellar surface phenomenon bears a striking resemblance to the capping phenomenon that has been described in numerous mammalian cell types. However, it occurs on a structure (the flagellum) that lacks most of the cytoskeletal components generally associated with capping in other systems. The FMG-1 monoclonal antibody inhibits flagellar surface motility visualized as the rapid, bidirectional translocation of polystyrene microspheres.

scholarly journals Concanavalin-A Induces Granulosa Cell Death and Inhibits FSH-Mediated Follicular Growth and Ovarian Maturation in Female Rats

Endocrinology ◽  
2013 ◽  
Vol 154 (5) ◽  
pp. 1885-1896 ◽  
Author(s):  
Ethel V. Velasquez ◽  
Mariana Ríos ◽  
María Elena Ortiz ◽  
Carlos Lizama ◽  
Elizabeth Nuñez ◽  
...  
Keyword(s):  
Cell Death ◽  
Granulosa Cell ◽  
Granulosa Cells ◽  
Concanavalin A ◽  
Ex Vivo ◽  
Female Rats ◽  
Carbohydrate Binding ◽  
Con A ◽  
Follicular Maturation

Abstract Reproductive success stems from a finely regulated balance between follicular maturation and atresia, in which the role of carbohydrate structure is poorly understood. Here, we describe for the first time a fraction of purified recombinant human FSH that is capable of bringing about the cell death of granulosa cells and preventing follicular maturation in a rat model. Further analysis by mass spectrometry revealed the presence of the lectin Concanavalin-A (Con-A) within this fraction of recombinant FSH. Using both the fractionated FSH and Con-A, the observed cell death was predominantly located to the granulosa cells. Ex vivo culture of rat follicles demonstrated that follicle degeneration occurred and resulted in the release of a denuded and deteriorated oocyte. Moreover, in vivo experiments confirmed an increase in atresia and a corresponding reduction confined to follicle in early antral stage. As a mechanism of action, Con-A reduces ovarian proliferation, Von Willebrand staining, and angiogenesis. Based on the observation that Con-A may induce granulosa cell death followed by follicle death, our results further demonstrate that follicular carbohydrate moiety is changing under the influence of FSH, which may allow a carbohydrate-binding lectin to increase granulosa cell death. The physiological consequences of circulating lectin-like molecules remain to be determined. However, our results suggest a potential exploitation of carbohydrate binding in fertility and ovarian cancer treatment. This work may shed light on a key role of carbohydrates in the still obscure physiological process of follicular selection and atresia.

Carbohydrate-binding specificity of concanavalin lectin from Canavalia spp.

2021 ◽  
Vol 16 (10) ◽  
pp. 27-32
Author(s):  
Geetha Suvarna ◽  
Bhagya B. Sharma ◽  
R. Sridhar Kandikere
Keyword(s):  
Specific Activity ◽  
Human Lymphocytes ◽  
Binding Specificity ◽  
Computational Method ◽  
Proliferation Index ◽  
Carbohydrate Binding ◽  
Ammonium Sulphate Precipitation ◽  
Sugar Derivatives ◽  
Mitogenic Potential ◽  
Seed Extracts

The carbohydrate-binding specificity of lectins from the four accessions of Canavalia seeds (C. ensiformis (ConA), C. cathartica (ConC), C. gladiata (ConG) and C. rosea (ConM) was studied by hemagglutination inhibition assay using monosaccharides, disaccharides and sugar derivatives. Canavalia seed extracts subjected to ammonium sulphate precipitation and the fraction with higher specific activity were analysed for carbohydrate-binding specificity and its mitogenic potential. All four lectins exhibited similar carbohydrate-binding specificity in agglutination inhibition which is in line with docking experiments. Dmannose and D-maltose were highly specific than other sugars. The results of computational method revealed differences in the affinity towards various carbohydrates. Mitogenic activity of all four lectins in human lymphocytes showed varied mitotic index. Among the four lectins studied, binding affinity to mannose and proliferation index was in the order ConG>ConA>ConM>ConC accounting to the efficacy of biological functions of highly similar analogues.

scholarly journals Posttranslational processing of concanavalin A precursors in jackbean cotyledons.

1986 ◽  
Vol 102 (4) ◽  
pp. 1284-1297 ◽  
Author(s):  
D J Bowles ◽  
S E Marcus ◽  
D J Pappin ◽  
J B Findlay ◽  
E Eliopoulos ◽  
...  
Keyword(s):  
Concanavalin A ◽  
Tertiary Structure ◽  
Peptide Bond ◽  
Distinct Species ◽  
Binding Activity ◽  
Carbohydrate Binding ◽  
Metabolic Labeling ◽  
Weak Bases ◽  
Processing Steps ◽  
Translational Product

Metabolic labeling of immature jackbean cotyledons with 14C-amino acids was used to determine the processing steps involved in the assembly of concanavalin A. Pulse-chase experiments and analyses of immunoprecipitated lectin forms indicated a complex series of events involving seven distinct species. The structural relatedness of all of the intermediate species was confirmed by two-dimensional mapping of 125I-tryptic peptides. An initial glycosylated precursor was deglycosylated and cleaved into smaller polypeptides, which subsequently reannealed over a period of 10-27 h. NH2-terminal sequencing of the abundant precursors confirmed that the intact subunit of concanavalin A was formed by the reannealing of two fragments, since the alignment of residues 1-118 and 119-237 was reversed in the final form of the lectin identified in the chase and the precursor first labeled. When the tissue was pulse-chased in the presence of monensin, processing of the glycosylated precursor was inhibited. The weak bases NH4Cl and chloroquine were without effect. Immunocytochemical studies showed that monensin treatment caused the accumulation of immunoreactive material at the cell surface and indicated that the ionophore had induced the secretion of a component normally destined for deposition within the protein bodies. Consideration of the tertiary structure of the glycosylated precursor and mature lectin showed that the entire series of processing events could occur without significant refolding of the initial translational product. Proteolytic events included removal of a peptide from the surface of the precursor molecule that connected the NH2- and COOH-termini of the mature protein. This processing activated the carbohydrate-binding activity of the lectin. The chase data suggest the occurrence of a simultaneous cleavage and formation of a peptide bond, raising the possibility that annealment of the fragments to give rise to the mature subunit involves a transpeptidation event rather than cleavage and subsequent religation.

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