Concanavalin A : [proceedings]
0
Citation
0
Reference
20
Related Paper
Abstract:
1 Concanavalin A: An Introduction.- I. Background Information.- II. Physical and Chemical Properties of Concanavalin A.- III. Biological Properties of Concanavalin A.- References.- 2 Structure and Function of Concanavalin A.- Abstract.- I. Introduction.- II. Structure of Concanavalin A.- III. Saccharide Binding Function of Concanavalin A.- IV. Multivalent Nature of Con A.- V. A Model for Interactions between Cell Surface Receptors and Cytoplasmic Structures.- References.- 3 Studies on the Combining Sites of Concanavalin A.- Abstract.- I. Introduction.- II. Methods, Results, and Discussion.- References.- 4 13C NMR Studies of the Interaction of Concanavalin A with Saccharides.- Abstract.- I. Introduction.- II. Methods.- III. Results and Discussion.- References.- 5 Self-Association, Conformation and Binding Equilibria of Concanavalin A.- Abstract.- I. Introduction.- II. Methods, Results, and Discussion.- III. Conclusion.- References.- 6 Studies on the Interaction of Concanavalin A with Glycoproteins.- Abstract.- I. Introduction.- II. Methods.- III. Results.- References.- 7 Interaction of Concanavalin A with the Surface of Virus - Infected Cells.- Abstract.- I. Introduction.- II. Methods, Results, and Discussions.- References.- 8 Concanavalin A as A Quantitative and Ultrastructural Probe for Normal and Neoplastic Cell Surfaces.- Abstract.- I. Introduction.- II. Methods.- III. Results and Discussion.- References.- 9 Microtubular Proteins and Concanavalin A Receptors.- Abstract.- I. Introduction.- II. Methods.- III. Results.- IV. Discussion.- References.- 10 Effects of Concanavalin a on Cellular Dynamics and Membrane Transport.- Abstract.- I. Introduction.- II. Methods of Procedure.- III. Results.- IV. Discussion.- References.- 11 The Characteristics of Succinylated Con a Induced Growth Inhibition of 3T3 Cells in Tissue Culture.- Abstract.- I. Introduction.- II. Methods.- III. Results.- IV. Discussion.- References.- 12 Cell Cycle Dependent Agglutinability, Distribution of Concanavalin a Binding Sites and Surface Morphology of Normal and Transformed Fibroblasts.- Abstract.- I. Introduction.- II. Materials and Methods.- III. Results.- IV. Discussion.- References.- 13 Concanavalin A and Other Lectins in the Study of Tumor Cell Surface Organization.- Abstract.- I. Introduction.- II. Methods.- III. Results.- IV. Discussion.- References.- 14 Modification of the Biological Activities of Concanavalin A by Anti-Concanavalin A.- Abstract.- I. Introduction.- II. Methods, Results, and Discussion.- References.- 15 Concanavalin A as A Probe for Studying the Mechanism of Metabolic Stimulation of Leukocytes.- Abstract.- I. Introduction.- II. Materials and Methods.- III. Results.- IV. Discussion.- References.- 16 Enhanced Cytotoxicity in Mice of Combinations of Concanavalin A and Selected Antitumor Drugs.- Abstract.- I. Introduction.- II. Materials and Methods.- III. Results.- IV. Discussion.- References.- 17 Effect of Concanavalin A and Phytohemagglutinin on the Modification of Immunogenicity of Canine Kidney Allografts.- Abstract.- I. Introduction.- II. Materials and Methods.- III. Results.- IV. Discussion.- References.- Abstracts.- Evidence for Conformational Changes in Concanavalin A upon Binding of Saccharides as Determined from Solvent Water Proton Magnetic Relaxation Rate Dispersion Measurements.- Magnetic Resonance Studies of Concanavalin A: Location of The Binding Site of Methyl-D-Mannopyranoside.- The Metal Ion Requirements of Concanavalin A.- The Kinetics of Cellular Commitment during Stimulation of Lymphocytes by Concanavalin A.- Isolation of A Glycoprotein Receptor for Concanavalin A from the Outer Surface of Mouse L Cells.- Electron Microscopic Study on Interaction of Concanavalin A with Mouse Lymphosarcoma Cells in Tissue Culture and in Ascites form.- The Effect of Glutaraldehyde Fixation on the Agglutination of Human Erythrocytes by Concanavalin A and Soybean Agglutinin.- Altered Net Cation Transfer Across the Ehrlich Mouse Ascites Tumor Cell During Exposure to Concanavalin A.- Effects of Con A on Frog Nerve and Muscle.- Modification of the Surface Characteristics of Developing Hemopoietic Cells from Normal Human Bone Marrow Revealed Ultrastructurally by the Concanavalin A-Peroxidasediaminobenzidine Technique.- Effects of Succinyl-Con A on the Growth of Normal and Transformed Mouse Fibroblasts.- Endotoxin-Like Activities in Concanavalin A Preparations.- Concanavalin A Induced Inflammation.- Enhanced Immunogenicity of Con A Coated El-4 Leukemia Cells.- List of Contributors.Cite
Cite
Citations (15)
Pronase
Thymocyte
Cite
Citations (30)
Cite
Citations (0)
Agglutination (biology)
Cite
Citations (21)
Synaptic junctional complexes from rat brain contain three major classes of glycoproteins which react with concanavalin A. They have apparent molecular weights of 110 000 (GP 110) 130 000 (GP 130), and 180 000 (GP 180). They are present in postsynaptic densities but are not found in microsomes, axolemma, synaptic vesicles, or myelin and are present in low concentrations in the Triton X-100 extract obtained during the preparation of synaptic junctions suggesting that they are uniquely localized to the postsynaptic apparatus. Reaction of the individual glycoproteins, partially purified by affinity chromatography on concanavalin A – agarose followed by polyacrylamide gel electrophoresis, showed that GP 130 contained the most receptor sites for concanavalin A per unit of protein followed by GP 180 and GP 110. Of the receptor sites for concanavalin A, 60–70% were subject to hydrolysis by endoglycosidase H indicating that the lectin reacts primarily with polymannose asparagine linked oligosaccharides. Each of the glycoproteins also reacted to varying degrees with the lectins from Lotus tetragonolobus (specific for α-L-fucose), wheat germ (N′-acetyl-D-glucosamine and (or) sialic acid), and lentils (mannose, N′-acetyl-D-glucosamine). Chromatography of 125 I-labelled concanavalin A positive glycoproteins on wheat germ Sepharose resolved GP 110 and GP 180 into wheat germ positive and negative components indicating the presence of some structural heterogeneity within these molecular weight classes.
Cite
Citations (56)
Agglutination (biology)
Cite
Citations (9)
Redistribution
Cell membrane
Cite
Citations (5)
Agglutination (biology)
Cite
Citations (202)
We have measured the quantitative binding of the radioactively labeled agglutinin (125)I-concanavalin A to normal mammalian cells and simian virus 40- and polyoma virus-transformed cells from tissue culture. Parallel measurements of the amount of (125)I-concanavalin A necessary to cause agglutination of the cells in suspension were carried out. The transformed and nontransformed cells used for these experiments show large differences in their ability to be agglutinated by (125)I-concanavalin A. However, these cell lines have the same number of specific binding sites and similar affinities for the agglutinin whether transformed, trypsinized, or nontransformed. We conclude that the differential capacity of concanavalin A to agglutinate transformed cells relative to normal cells does not result from differences in the number of binding sites between the two types of cells.
Trypsinization
Agglutination (biology)
Cite
Citations (118)