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Tuesday, July 28, 2020 | History

2 edition of study of concanavalin A induced agglutination based on a crosslinked dextran gel model system found in the catalog.

study of concanavalin A induced agglutination based on a crosslinked dextran gel model system

Donald William Evans

study of concanavalin A induced agglutination based on a crosslinked dextran gel model system

by Donald William Evans

  • 233 Want to read
  • 27 Currently reading

Published by s.n.] in [Toronto .
Written in English

    Subjects:
  • Agglutination -- Mathematical models,
  • Concanavalin A.,
  • Molecular biology -- Mathematical models

  • Edition Notes

    Statementby Donald William Evans.
    ContributionsToronto, Ont. University.
    The Physical Object
    Paginationxvii, 293 p. :
    Number of Pages293
    ID Numbers
    Open LibraryOL19894370M

      NC37 and KB cells grown in suspension culture remained agglutinable at 23° C by concanavalin A (Con A) after sufficient glutaraldehyde fixation to prevent lateral mobility (clustering) of Con A binding sites. In contrast, at 4° C agglutination of the fixed cells was by: 2. A-dependent agglutination (5). Characterization of rod cell agglutination by Con A. Con A-dependent agglutination of intact rod cells of ONT-3 and ONS-2 was studied in comparison with the spheroplast agglutination of W by Con A (5). Atime course study revealed that the rod cell aggluti-nation proceeded at a considerably more rapid rate and.

    Abstract. The initial event in the biological activity of concanavalin A (Con A) involves binding of the protein to cell surface receptors. The nature and mechanism whereby such binding may occur is described in terms of cell surface carbohydrates and the demonstrated specificity of the by: Start studying blood groups. Learn vocabulary, terms, and more with flashcards, games, and other study tools.

      Concanavalin A markedly agglutinated isolated epithelial cells from the intestine of the human fetus but not from the intestine of the adult. Wheat germ agglutinin only moderately agglutinated cells from the intestine of an adult. These results extend the studies of concanavalin A agglutination of embryonic cells to human tissue, and they suggest that concanavalin A may be reacting with a Cited by: Abstract. Agglutination of human erythrocytes by the lectin concanavalin A is enhanced when the erythrocytes are pretreated with neuraminidase, which removes sialic acids, or with pronase, which degrades both the glycophorins and band 3 by: 7.


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Study of concanavalin A induced agglutination based on a crosslinked dextran gel model system by Donald William Evans Download PDF EPUB FB2

Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected by: Summary Candida albicans cells were treated with alkali and acid to extract preferentially the cell wall α-mannan.

Cells were recovered at three stages, as extraction proceeded from mild to more extensive: Alk-1, Alk-2 and Alk + Acid. Yeast adhesion to human epithelial cells was then examined with an in-vitro adherence assay. Yeasts from all three stages of extraction adhered in significantly Cited by: Furthermore, human erythrocytes, which are not normally agglutinated by concanavalin A, became agglutinable by the lectin when the erythrocytes were preincubated with purified galactosyltransferase.

These experiments suggest a direct and possible specific role of cell surface galactosyltransferase enzyme in the mechanism of concanavalin A agglutination of by:   The dependence of agglutination on cell metabolism was studied: cold (4 degrees C), sodium azide (15 mM) and cytochalasin B (10 micrograms/ml) inhibited thymocyte adhesion.

The importance of lateral movements of ConA molecules was assayed by measuring the adhesion of ConA-coated glutaraldehyde-fixed thymocytes to untreated cells: substantial binding occurred, but at a reduced level relative to untreated by: " Con A gave strong agglutination reaction with pathogenic strains of Entamoeba histolytica while there was little or no reaction with non-pathogenic strains.

Thus this method may be used in differentiating pathogenic and non-pathogenic strains in vitro. Pathogenic and non-pathogenic species of small free-living amoebae could not be differentiated on the basis of con A agglutination reaction Cited by: 1.

In this study, the successful acrylic derivatization of dextran and concanavalin A (con A) to form dextran methacrylate and con A methacrylamide is shown. To determine changes in the surface membrane of granulosa cells related to follicular atresia and luteinization, their agglutination behavior with Concanavalin A has been studied by quantitative by: 1.

The significance of the sharp break in the Arrhenius plot observed for the concanavalin A-dextran interaction in this study as well as for the lectin-mediated cell agglutination reported earlier. The sensitive fluid is based on the competitive binding of glucose and dextran with a glucose-specific binding protein, Concanavalin A.

Basically, the sensor is filled with the sensitive fluid. The agglutinability of rat C 6 glioma cells by concanavalin A (Con A) depends upon cell density. From sparse density to near confluency agglutinability increases as cell density rises.

Both the half-maximal concentration and the maximum amplitude of agglutination by Con A are functions of cell density, but are separate cell parameters differing in the extent to which they are affected by Cited by: " Concanavalin A (Con A) agglutinated all Naegleria gruben strains tested but did not agglutinate any N.

fowleri strains tested. Agglutination was time and temperature dependent and Con A concentration and amoeba concentration dependent over certain ranges. Agglutination increased to maximum up to l h incubation with Con A. At least 1 X amebae/ml were needed for maximum agglutination, and Cited by: of Concanavalin A from the seeds of Canavalia ensiformis” is the original work carried out by me under the supervision of Dr.

Sujit K. Bhutia, Assistant Professor, Department of Life Science, National Institute of Technology Rourkela (NITR) and to the best of my knowledge and belief the.

Concanavalin A-induced agglutination of human leukemic and lymphoma cells. Maca RD. With a newly developed turbidometric method, concanavalin A was shown to agglutinate normal lymphocytes, lymphoma cells, and leukemic cells from chronic lymphocytic leukemia and from acute myelocytic and lymphocytic by: 2.

Heparin and concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity. A study on concanavalin a binding to human erythrocytes.

The effect of diabetes on hepatocyte plasma membrane fluidity and concanavalin A-induced agglutination. Experimental Cell Research(1), DOI: / Cited by:   The Concanavalin A (Con A) model is a typical and well established model for investigating T-cell and macrophage dependent liver injury in mice, which closely mimics the pathogenesis mechanisms and pathological changes of patients, and is regarded as the best experimental model for AIH research so by:   With much foresight, they suggested that the hemagglutination induced by concanavalin A might be a consequence of a reaction of the plant protein with carbohydrates on the surface of the red cells.

Already the early results obtained by Stillmark indicated some selectivity in the ricin-induced agglutination of red cells from different by: binding of concanavalin A (Con A) to the cell surface was very specific and the available binding sites were saturated withi a fewn minutes.

The amoun of tI-Con A boun tdo EATC was x io7 molecules/cell at 37 °C and x io7 molecules/cell at o °C. Under these conditions, cell agglutination was observe at 37d ° onlC an noyd t at o °C.

Microgels consisting of dextran derivatives cross-linked with the lectin concanavalin A (ConA) have been incorporated with insulin [, ]. It was observed that the insulin was released in. The assay system used to assess cell agglutination also seems to be important, since many laboratories studying the same agglutination reaction have reported dissimilar or contradictory results.

To provide further information on the molecular mechanism of agglutination we have begun a systematic study on the aggregation of human red cells by the lectin concanavalin A (Con A).Cited by: Erythrocytes of normal Wistar rats are maximally agglutinated at μg/ml concanavalin A (Con A). In rats bearing Yoshida ascites tumor (i.

p.), however, the red cells in circulation and those contaminating the tumor fluid agglutinate the most at 50 μg/ml of the lectin. The enhanced agglutinability of circulatory RBCs arises 3 days after tumor transplantation, but the erythrocytes in the Cited by: 1.

Glucose-responsive systems are very useful for self-regulated insulin delivery. In this study, glucose-responsive composite microparticles based on chitosan, concanavalin A and dextran were.N-butyl-N-(4-hydroxybutyl)nitrosamine (BBN), which is a potent, specific bladder carcinogen in rats, and its related compounds were orally administered to rats for 1 bladder cells were isolated by the treatment with EDTA and sonication and they were subjected to agglutination assay by concanavalin Cited by: 4.Concanavalin A markedly agglutinated isolated epithelial cells from the intestine of the human fetus but not from the intestine of the adult.

Wheat germ agglutinin only moderately agglutinated cells from the intestine of an adult. These results extend the studies of concanavalin A agglutination of embryonic cells to human tissue, and they suggest that concanavalin A may be reacting with a Cited by: