Interaction Of Concanavalin Research Articles

Effects of hydroxyl compounds on the interaction of Concanavalin A with polysaccharides

Effects of hydroxyl compounds on the interaction of Concanavalin A with polysaccharides

Ultraviolet difference spectral studies on concanavalin A. Carbohydrate interaction.

The interaction of concanavalin A, the phytohemagglutinin of the jack bean, with a variety of glycosides has been studied by the technique of ultraviolet difference spectroscopy. Whereas methyl α‐d‐gluco‐ and manno‐pyranoside gave rise to relatively low intensity difference spectra, p‐nitrophenyl α‐d‐mannopyranoside and α‐d‐glucopyranoside yielded large difference spectra upon interaction with concanavalin A. Using this technique as a measure of concanavalin A activity, it was demonstrated that the protein specifically binds low molecular weight carbohydrates at much lower pH values (e. g. pH 2.4) than previously believed. Although polysaccharides are also bound at these low pH values, they are not precipitated by concanavalin A. Molecular weight studies in acid media indicate that the protein does not dissociate and it is suggested that electrostatic repulsion of the protein molecules due to their high net positive charge prevents protein‐polysaccharide lattice formation and hence failure of the complex to precipitate.

Interaction of concanavalin A with an arabinogalactan from the cell wall of Mycobacterium bovis.

The arabinogalactan isolated from the cell wall of Mycobacterium bovis reacts to form a precipitate with concanavalin A, the phytohemagglutinin of the jack bean. A typical precipitin-like curve is obtained when increasing amounts of the polysaccharide are added to a constant quantity of concanavalin A. Inhibitor studies suggest that concanavalin A reacts with the arabinogalactan by interacting with the C-2, C-3, and C-5 hydroxyl groups of the alpha-d-arabinofuranosyl residues situated at the chain ends of this polysaccharide.

Interaction of concanavalin A with polysaccharides of salmonellae

Interaction of concanavalin A with polysaccharides of salmonellae

Interaction of concanavalin A with polysaccharides of salmonellae

Interaction of concanavalin A with polysaccharides of salmonellae

The interaction of concanavalin A with methyl α- D-glucopyranoside

The interaction of concanavalin A with methyl α- D-glucopyranoside

Protein-Carbohydrate Interaction: XIII. THE INTERACTION OF CONCANAVALIN A WITH α-MANNANS FROM A VARIETY OF MICROORGANISMS

Abstract The interaction of concanavalin A with α-mannans from several species of microorganisms has been studied by the techniques of quantitative precipitation and hapten inhibition. Similar to concanavalin A-dextran precipitation, the reaction between concanavalin A and yeast mannan (Saccharomyces cerevisiae) is optimal near neutrality (pH 5.7 to 6.7). Among the polysaccharides which form a precipitate with concanavalin A, i.e. glycogens, amylopectins, mannans, dextrans, and levans, mannans appear to be the most reactive. This is illustrated by hapten inhibition studies conducted on the concanavalin A-mannan system wherein relatively larger amounts of inhibitors are required to effect the same percentage inhibition as concanavalin A-dextran or concanavalin A-levan precipitation. The inhibition of a number of mannose-containing oligosaccharides has been examined, and data are presented which suggest that the concanavalin A-combining sites may be more extensive than hitherto believed, and may, in fact, be complementary to a sequence of several α-(1 → 2)-d-mannopyranosyl residues.

Protein-carbohydrate interaction: XVI. The interaction of concanavalin A with dextrans from L. mesenteroides B-512-F, L. mesenteroides (Birmingham), Streptococcus bovis, and a synthetic α-(1 → 6)- d-glucan

The precipitation reaction between concanavalin A, the jack-bean hemagglutinin and several dextrans has been examined by means of the quantitative precipitin technique. A synthetic linear α-(1 → 6)- d-glucan did not form a precipitate with concanavalin A, demonstrating that only branched α- d-glucans precipitate with the protein. The dextran from Streptcoccus bovis produced a typical precipitation curve with concanavalin A and gave the disaccharide nigerose when subjected to acetolysis. On the basis of these data it is suggested that this dextran, hitherto believed to be linear, is in fact a branched polymer. The concanavalin A precipitation curves of the dextrans from Leuconostoc mesenteroides NRRL B-512-F and Betacoccus arabinosaceous ( L. mesenteroides) Birmingham strain were compared with the S. bovis dextran and an attempt has been made to correlate these data with the molecular structures of these dextrans. The differences in the solubility of the dextran-concanavalin A precipitates and the relative ease of inhibition of these systems in the presence of hapten inhibitor are also discussed.

CORRECTIONS- Protein-Carbohydrate Interaction. XX. The Interaction of Concanavalin A with Sophorose and Some of Its Derivatives

CORRECTIONS- Protein-Carbohydrate Interaction. XX. The Interaction of Concanavalin A with Sophorose and Some of Its Derivatives

Protein-carbohydrate interaction. XX. The interaction of concanavalin A with sophorose and some of its derivatives.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProtein-Carbohydrate Interaction. XX. The Interaction of Concanavalin A with Sophorose and Some of Its Derivatives*I. J. Goldstein, R. N. Iyer, E. E. Smith, and L. L. SoCite this: Biochemistry 1967, 6, 8, 2373–2377Publication Date (Print):August 1, 1967Publication History Published online1 May 2002Published inissue 1 August 1967https://doi.org/10.1021/bi00860a012RIGHTS & PERMISSIONSArticle Views123Altmetric-Citations50LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (504 KB) Get e-Alerts Get e-Alerts

Protein-carbohydrate interaction : VIII. A turbidimetric method for the analysis of D-mannose

A unique, spectrophotometric method for the quantitative of D-mannose in the presence of other sugars is described. The procedure depends on the degree to which the turbidity formed on interaction of concanavalin A with glycogen is specifically inhibited by D-mannose. The analysis, whose useful is 300 to 750 μg/ml, gives essentially the same result as other methods commonly used. A correction for the presence of D-glucose, which also inhibits glycogen-concanavalin A interaction, is readily achieved by use of the Glucostat reagent.

Interaction of concanavalin A, a phytohemagglutinin, with model substrates

Interaction of concanavalin A, a phytohemagglutinin, with model substrates