Concanavalin A by Tushar Chowdhury

Cover of: Concanavalin A | Tushar Chowdhury

Published by Springer .

Written in English

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Subjects:

  • Life Sciences - Biochemistry,
  • Life Sciences - Zoology - General,
  • Science / Zoology,
  • Science,
  • Congresses

Edition Notes

Advances in Experimental Medicine & Biology

Book details

The Physical Object
FormatHardcover
Number of Pages360
ID Numbers
Open LibraryOL9401338M
ISBN 100306390558
ISBN 109780306390555

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Concanavalin A is a tetrameric protein with four identical 28 kDa subunits. 29 The minimal structure exhibiting high affinity binding of carbohydrates is the dimeric form. The dimer form of ConA is an active stable structure, and the tetramer–dimer transition can be promoted by low pH or succinylation of the protein.

30 For reasons of economy. Concanavalin A (Con A), a plant lectin, has become an object of extensive research not only for the biochemist, but also for the bi­ ologist, biophysicist, pathologist, immunologist and others. On Aprila group of scholars from four continents met on the campus of the University of Oklahoma for an International Symposium on Con : Tushar Chowdhury.

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Sample Content; Standard Article. Concanavalin A. Part 3. Manganese. A Joseph Kalb (Gilboa) 1, John R Helliwell 2; Published. Concanavalin A (Con A), a plant lectin, has become an object of extensive research not only for the biochemist, but also for the bi­ ologist, biophysicist, pathologist, immunologist and others.

On Aprila group of scholars from four continents met on the campus of the University of. ISBN: OCLC Number: Description: 1 online resource: Contents: 1 Concanavalin A: An Introduction --I. Background Information al and Chemical Properties of Concanavalin A ical Properties of Concanavalin A --References Structure and Function of Concanavalin A --Abstract --I.

Concanavalin A: [proceedings]. [Tushar K Chowdhury; Adolph Kurt Weiss;] -- Concanavalin A (Con A), a plant lectin, has become an object of extensive research not only for the biochemist, but also for the biologist, biophysicist, pathologist, immunologist and others.

The newcomer to this area will find that a careful study of this book will. Concanavalin A (Con A), a plant lectin, has become an object of extensive research not only for the biochemist, but also for the bi­ ologist, biophysicist, pathologist, immunologist and others.

On Aprila group of scholars from four continents met on the campus of the University of Oklahoma for an International Symposium on Con A. concanavalin: [ kon″kah-nav´ah-lin ] a lectin isolated from the jack bean (Canavalia ensiformis) that agglutinates mammalian erythrocytes and is a mitogen that stimulates predominantly T lymphocytes.

Abbreviated ConA. The intravenous injection of the plant lectin concanavalin A (ConA) is a widely used model for acute immune-mediated hepatitis in mice.

In contrast to several other models for acute hepatic damage, ConA-induced injury is primarily driven by the activation and recruitment of T cells to the liver. Hence, the ConA model has Concanavalin A book features with Cited by: C.A.S.: First crystallized by Sumner and Howell (), Concanavalin A (ConA) has proven to be an interesting and useful lectin.

Lectins are proteins that react with specific terminal sugar residues and are useful probes in studying carbohydrates of cell surfaces. Concanavalin A also contains many residues essential to the recognition and binding of carbohydrate ligands.

The c arbohydrate binding site is comprised of Tyr, Pro, Asn, Thr, Asp, Leu, Asp, and Arg, a conserved sequence in the legume lectin family (2). Of particular interest is the circular permutation of Concanavalin. Concanavalin A from Canavalia ensiformis (Jack bean) Product Number C Storage Temperature -0 °C Product Description CAS Number: Molecular Weight: The monomeric molecular weight is kDa.

At pH Con A exists as a dimer and at pH>7 it exists as a tetramer.1 Extinction Coefficient: E1% = ( nm, mM NaCl)2 pI: Abstract. Interactions between concanavalin A and cell wall digests of Bacillus subtilis resulted in insoluble complexes as observed by double gel diffusion, turbidity, and analysis of the precipitate.

The macromolecular constituent of the cell walls complexing with concanavalin A was the polyglucosylglycerol phosphate teichoic by: Targeting Tumor via Novel Drug Delivery System: Concanavalin-A conjugated Solid Lipid Nanoparticles bearing Mitoxantrone for Tumor Targeting [Mahor, Alok, Jain, S.

K., Prajapati, S. K.] on *FREE* shipping on qualifying offers. Targeting Tumor via Novel Drug Delivery System: Concanavalin-A conjugated Solid Lipid Nanoparticles bearing Mitoxantrone for Tumor Price: $ Answers to all problems are at the end of this book.

Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Using the Active Model for concanavalin A, discuss an example in which a difference in protein primary structure leads (o a difference in protein function.

Canavalin is a plant protein found in the jack bean, sword bean, and related is the major storage protein found in these plants' seeds, and is one of four proteins readily isolated from the seeds; the others are concanavalin A, concanavalin B, and urease.

Canavalin is a vicilin protein homologous to phaseolin. The crystallization of jack bean seed proteins has been studied. Annabi, "Concanavalin-A triggers inflammatory response through JAK/STAT3 signalling and modulates MT1-MMP regulation of COX-2 in mesenchymal stromal cells,".

This volume surveys the chemistry, biochemistry, biosynthesis, metabolism and pharmacological properties of lectins. Lectins, which are most commonly found in plants, are widespread natural products with striking biological activities.

Their specific ability to recognise and bind to simple or complex saccharides facilitates their role as effective information protein molecules.4/5(1). Sumner and his associates were the first group to isolate an agglutinin in relatively pure form (a).

They were able to crystalize a lectin from the jack bean (Canavalia ensiformis) and referred to it as concanavalin fraction A. This particular fraction of the jack bean later became known as concanavalin A or simply as Con by: 3.

Concanavalin A Slide Coating Protocol. Introduction. We initially developed a slide coating method using Concanavlin A, a prototypical lectin that binds glycosul and mannosyl groups. Although we favor custom made slides from Erie Scientific for our arrays, home made slides can be easily made for small scale experiments.

ConA (Concanavalin A) Affinity Chromatography REFERENCES: Pharmacia-LKB notes on the resin; Pharmacia book on Affinity Chromatography; for the structure of mannopyranose and methyl-glucopyranoside, see Morrison & Boyd, Organic Chemistry (in the 3rd edition, see pages ). Concanavalin A is a lectin (typically obtained from wheat germ).

It is able to bind. Con A recognizes α-linked mannose present as part of a “core oligosaccharide” in many serum and membrane glycoproteins. Biotinylated Concanavalin A has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin.

This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide. Concanavalin-coated coverslips. Make stock 5 mg/mL solution (add 1 mL sterile PBS to bottle – gently rotate to mix) Keep sterile - work in sterile hood; aliquot µL into microfuge tubes (cannot take repeated freeze-thaw cycles) Coat coverslip bottom dishes with mL mg/mL: mL (5 mg/mL) + mL PBS.

Concanavalin A; References; Images; Concanavalin A (PDB ID: 3D4K) Created by Jacqueline Stevens C oncanavalin A (ConA), a legume lectin isolated from Canavalia ensiformis, is a sugar-binding protein (1).Plant lectins such as ConA contain at least one noncatalytic domain that binds reversibly to mono saccharide or oligosaccharide ligands (8).

The molecular weight and. One of the core principles of a Paleo diet is avoiding foods that contain compounds called toxic term toxic lectin originates from the fact that lectins are a class of carbohydrate-binding proteins found in all foods (and indeed all forms of life, including humans!), but that only a subset of these are an issue for human health via food consumption.

antinutritional protein, concanavalin A, is somewhat protected from heat treatment (Udedibie and Carlini, ). Even minute amounts of this proteinmay be harmful to animals. Cover crop/green manure: As a cover crop jack bean produces phytochemicals that act as a pesticide, bactericide, and a fungicide (Morris, ).

The canopyFile Size: KB. This Concanavalin A product is supplied as an aseptically filled, lyophilized powder, which has been γ-irradiated. This Con A product agglutinates 2% fresh human type A red blood cells in M Phosphate Buffered Saline containing calcium and manganese, pH at ≤64 µg lectin/ml.

The mitogenic property of this lectin was confirmed by. concanavalin - find the meaning and all words formed with concanavalin, anagrams with concanavalin and much more. High purity Concanavalin A (Con A) lectin has a highly specific carbohydrate binding affinity, for research and in vitro diagnostic analysis.

Affinity purified, lyophilised powder. Con A is not blood group specific, has an affinity for terminal α-D-mannose and α-D-glucose residues and requires the presence of Ca 2 + and Mn 2 + for activity. A novel fluorescent concanavalin A detection platform using an anti-concanavalin A aptamer and graphene oxide H.

Liu, Y. Bai, J. Qin, Z. Chen and F. Feng, Anal. Methods,9, Concanavalin A (Con A) is one of the most widely used lectins in cell biology.

Our tetramethylrhodamine conjugate of Con A exhibits the bright, orange-red fluorescence of tetramethylrhodamine (absorption/emission maxima ~/ nm). Tetramethylrhodamine Con A selectively binds to α-mannopyranosyl and α-glucopyranosyl residues.

Concanavalin A (Con A) can induce well known AIH in mice that mimics the pathological picture and underling immune mechanisms of AIH patients (Wang. Concanavalin A as a Tool. Edited by H. Bittiger and H. Schnebli. xv + (Wiley-Interscience: London and New York, October ) £; $ Title: Concanavalin A, from an Old Protein to Novel Candidate Anti-Neoplastic Drug VOLUME: 3 ISSUE: 3 Author(s):Chun-Yang Li, Huai-Long Xu, Bo Liu and Jin-Ku Bao Affiliation:School of Life Sciences, Sichuan University, ChengduChina.

Keywords:Apoptosis, autophagy, cancer, concanavalin A (ConA), legume lectin, plant lectin, carbohydrate-binding proteins, (ConA), Cited by: The characteristics of canine ILproducing cells are incompletely understood.

Expression of mRNA encoding orthologs of IL and the IL receptor has been documented in tissues from dogs with arthritis, inflammatory bowel disease, and lymphoma; however, no associations have been found between IL gene expression and disease phenotype in these by: 5.

The Covalent and Three-Dimensional Structure of Concanavalin A III. STRUCTURE OF THE MONOMER AND ITS INTERACTIONS WITH METALS AND SACCHARIDES* (Received for publication, J ) JOSEPH W.

BECKER, GEORGE N. REEKE, JR., JOHN L. WANG, BRUCE A. CUNNINGHAM, AND GERALD M. EDELMAN From The Rockefeller University. Glycan – Concanavalin A (Con A) Ligand: Glycan. Analyte: Concanavalin A (Con A) k on = e3 1/M.

k off = e-3 1/s. K D = μM. DOWNLOAD APP NOTE. BOOK DEMO. Overview. OpenSPR is the world’s only benchtop surface plasmon resonance (SPR) instrument. It provides high quality, label-free interaction analysis for a fraction of.

The metal binding sites of the concanavalin A are situated in the amino terminal part of the polypeptide chain. In this lectin, each subunit has aspartic 10 asparag histid ser glutamic acid 8, and tyrosine 12 that are involved in the binding to one calcium and one magnesium ion. Alpha-amanitin-concanavalin A conjugates as inhibitors of specific cell types / By.

Hencin, Ronald Stephen, Type. Book Material. Published material. Publication info. Notes: Typescript. Vita. Thesis--University of Florida. Subjects. Available in the National Library of Australia collection. Author: International Symposium on Concanavalin A, Norman, Okla., ; Format: Book; xiii, p.: ill.

InJames B. Sumner at Cornell University (Ithaca, New York), well known for being the first to crystallize in an enzyme, urease (for which he was awarded the Nobel Prize 21 years later), isolated from jack bean (Canavalia ensiformis) a crystalline protein that he named concanavalin A and in this way obtained a pure hemagglutinin for Cited by: Concanavalin A (Con A) induced suppressor cell activity was evaluated in a group of ovine progressive pneumonia virus-antibody positive sheep (OPPV+).Zhankuic acid A as a novel JAK2 inhibitor for the treatment of Concanavalin A- induced hepatitis.

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