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Monday, November 30, 2020 | History

2 edition of Effects of divalent metal ions on the binding of saccharides to concanavalin A found in the catalog.

Effects of divalent metal ions on the binding of saccharides to concanavalin A

Douglas James Christie

Effects of divalent metal ions on the binding of saccharides to concanavalin A

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  • 20 Currently reading

Published .
Written in English

    Subjects:
  • Concanavalin A.,
  • Metal ions.

  • Edition Notes

    Statementby Douglas James Christie.
    The Physical Object
    Paginationviii, 53 leaves :
    Number of Pages53
    ID Numbers
    Open LibraryOL16444644M

    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. @article{osti_, title = {Interaction of calcium with the human divalent metal-ion transporter-1}, author = {Shawki, Ali and Mackenzie, Bryan}, abstractNote = {Iron deficiency is the most prevalent micronutrient deficiency worldwide. Whereas dietary calcium is known to reduce the bioavailability of iron, the molecular basis of this interaction is not understood.


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Effects of divalent metal ions on the binding of saccharides to concanavalin A by Douglas James Christie Download PDF EPUB FB2

Addition of Ni2+ and of Ca2+ confers on concanavalin A high resistance towards proteolytic attack so that even after long periods of exposure to the enzymes, almost all of the saccharide-binding capacity is preserved.

Ni2+ alone protects strongly at pH but not at pH Cited by:   Demetallized concanavalin A is degraded rapidly at pH and by α-chymotrypsin, thermolysin or trypsin, yielding peptide fragments devoid of abil Cited by: Tetracycline is one of the most commonly used antibiotics in the world.

Eventually, large amounts of this contaminant will enter into the subsurface environment, where a variety of ions exist. In this study, the effects of divalent metal cations (Mg2+, Ca2+, Pb2+ and Cu2+) and inorganic anions (Cl−, NO3−, SOCited by: 7.

Concanavalin A (con A) is a saccharide-binding pro- tein of the Jack bean [ The protein contains two different metal-binding sites, which must be occupied in order for saccharide binding to be possible [2,3]. When the metal ions are removed by acid treatment. Each subunit contains two metal binding sites, one site (S2) which binds a Ca 2+ ion about Å from the center of the saccharide binding site and a second site (S1) which binds a Mn 2+ ion about Å from the center of the carbohydrate binding site.

Both metal ions can be removed and a Cd 2+ ion can be substituted into the S1 site as Cited by:   When the metal ions are removed by acid treatment, the demetallized protein can bind only divalent transi- tion metal ions (Mn2*, Co^, Ni2*, Zn^, or Cd2^ at a site designated S 1, but it cannot bind Ca2* or saccharide.

When Sl is occupied by one of the metal ions listed above, the protein can bind Ca2'1' at a second metal- binding site. A metal-binding region is, in fact, a double site consisting of a transition metal-binding site and a calcium-binding site bridged by a shared carboxyl group of an aspartic acid residue.

The transition metal-binding site can be populated by one of the divalent metal ions of the first transi- tion series as well as by Zn~2 and Cd~2 [12].

synergistic effects of Mg*+ and divalent transition metal ions are not observed (2). During an investigation of the regulation P-enolpyruvate carboxykinase by tryptophan (3), it was found that sulfate ion enhances the activity of this enzyme, but only in the presence.

It is of interest in this connection that HP in contrast to most mitogenic lectins lacks divalent metal ions.

SBA has recently also been found to contain divalent metal ions including Ca 2+ (unpublished). It is known that Ca 2+ plays an important role in cell activation (5,6).

The molecular structure of a triclinic crystal form of concanavalin A has been refined at A resolution. The crystals have unit cell dimensions a = A, b = A, c = A, alpha = Effect of carbohydrate and metal ion inding on the reactivity of the essential thiol groups of lima beam lectin.

binding to concanavalin A, saccharide was the most potent. of the divalent ions from lectin abolishes its sugar binding ability (24), although the divalent ions do not interact di-rectly with the saccharide as they do in calcium-dependent animal lectins (25). Despite the importance of metal ions in controlling the structural stability and the substrate bind.

Cite this chapter as: Sorokin V.A., Valeev V.A., Degtyar M.V., Gladchenko G.O., Blagoi Y.P. () Effects of divalent metal ions on secondary and tertiary structures. The effect of the sulfation pattern of saccharides on heavy metal binding preferences is enigmatic because the accessibility to structurally defined sulfated saccharides is limited and because standard analytical techniques cannot be used to quantify these interactions.

Effects of saccharide and salt binding on the dimer-tetramer equilibrium of concanavalin A. Biochemistry20 Saccharide binding to transition metal ion free concanavalin A. Biochemistry17 High-performance affinity chromatography of divalent concanavalin A on matrices of variable ligand density.

elements within the binding pocket suggest a general mode of divalent metal ion stabilization of this type of frameshifter pseudoknot. These results provide new thermodynamic and structural insights into the role divalent metal ions play in stabilizing RNA tertiary structural motifs such as pseudoknots.

# Academic Press. However, the effect of other divalent ions on cellulases activities seems to be variable among the enzymes secreted by different microorganisms (e.g., Table 1). The effect of divalent ions on cellulases is not well elucidated, and possibly occurs by redox effects on the amino acids, increasing or decreasing their activities [ 49 ].

The specific properties of the metal ions, however, probably have a more significant effect on the stabilities of the divalent metal complexes than the basicities of the ligands.

The Cu complexes of the P 3 O 10 and P 3 O 8 (NH) 2 ligands show the highest log 10 β ML values, as well as a similar r M dependence for the log 10 β ML values.

Divalent metal ions are effective counterions for neutralization of charges on phosphate groups and they occupy specific metal-binding sites. To clarify the contribution of divalent metal ions to RNA folding, we performed titrations in the presence of monovalent Na + cations.

Saccharide binding to transition metal ion free concanavalin A. Christie DJ, Alter GM, Magnuson AJ. Saccharide binding has been observed with demetallized concanavalin A in the presence of Ca(2+) only, using the fluorescent sugar 4-methylumbelliferyl alpha-D-mannopyranoside.

The affinity of the lectin Concanavalin A (Con A) for saccharides, and its requirement for metal ions such as Mn2+ and Ca2+, have been known for about 50 years.

Previous studies have also suggested that the removal of the divalent ions from lectin abolishes its sugar binding ability (24), although the divalent ions do not interact directly with the saccharide as they do in calcium-dependent animal lectins (25). Effect of divalent metal ions on the digestibility of concanavalin A by endopeptidases.

Blumberg S, Tal N. Demetallized concanavalin A is degraded rapidly at pH and by alpha-chymotrypsin, thermolysin or trypsin, yielding peptide fragments devoid of. To determine the effect of the divalent metal cation on the selective transfer of soluble saccharides, we replaced magnesium with calcium, which is known to have a greater binding affinity for palmitic acid.

Concentrations of each metal cation were selected to be representative of ocean conditions. This is one-half the molecular weight of concanavalin A in solution and is equal to the equivalent binding weight of concanavalin A for transition metal ions, calcium ions and α-methyl-d.

The effects of metal ions on heparin/HS-protein interactions in non-physiological concentrations. Citation: Fuming Zhang, Xinle Liang, Julie M Beaudet, Yujin Lee, Robert J Linhardt. () The effects of metal ions on heparin/heparin sulfate-protein interactions. J Biom Tech Res 1(1): The binding of carbohydrate substrates to concanavalin A (Canavalia ensiformis agglutinin (ConA)) is essential for its interaction with various glycoproteins.

Even though metal ions are known to control the sugar binding ability of legume lectins, the interplay between sugar and metal ion binding to ConA has not been elucidated in a detailed manner at the atomic level.

Ribulose-1,5-bisphosphate carboxylase-oxygenase is deactivated by removal of Mg++. The enzyme activities can be restored to a different extent by the addition of various divalent ions in the presence of CO2. Incubation with Mg++ and CO2 restores both enzyme activities, whereas, the treatment of the enzyme with the transition metal ions (Mn++, Co++, and Ni++) and CO2 fully reactivates the.

Retinal Vessel Integrity Fluorescein Labeled Concanavalin A, supplied by Vector Laboratories, used in various techniques. calcium or manganese ions at each of its four saccharide binding sites Although these divalent metal ions are bound tightly to the polypeptide structure buffers which can bind calcium such as phosphate generally should.

Fluorescein Labeled Concanavalin A, supplied by Vector Laboratories, used in various techniques. often present in the purest preparations due to hydrolytic damage within the seeds Con A requires calcium or manganese ions at each of its four saccharide binding sites Although these divalent metal ions are bound tightly to the polypeptide.

Interactions of saccharides with concanavalin A. Mechanism of binding of α- and β-methyl D-glucopyranoside to concanavalin A as determined by carbon nuclear magnetic resonance. Biochemistry12 (22), DOI: /bia Xiang. citation " IonCom is an ligand-specific method for small ligand (including metal and acid radical ions) binding site prediction.

Starting from given sequences or structures of the query proteins. Metal ion activation of saccharide binding has been studied for concana-valin A near pH Although two metal ions, a transition metal ion and a Ca 2+ ion, can bind, both are not required.

Ca 2+ alone, Mn 2+ alone, or Ca 2+ with other transition metal ions can activate this lectin. Only one Ca 2+ ion per subunit or only one Mn 2+ per subunit is sufficient. Metal ion binding was studied by. Abstract The effect of divalent metal ions on the activity of glycerophosphocholine cholinephosphodiesterse from ox brain was examined.

Zn(2+)- and Co(2+)-glycerophosphocholine cholinephosphodiesterases were prepared from the exposure of apoenzyme to Zn2+ and Co2+, respectively, and the properties of two metallo-phosphodiesterases were compared to those of native. ARTICLE OPEN Effect of divalent ions and a polyphosphate on composition, structure, and stiffness of simulated drinking water biofilms Yun Shen1,4, Pin Chieh Huang2, Conghui Huang 1, Peng Sun 1, Guillermo L.

Monroy2, Wenjing Wu1, Jie Lin, Rosa M. Espinosa-Marzal 1, Stephen A. Boppart 2,3, Wen-Tso Liu1 and Thanh H. Nguyen1 The biofilm chemical and physical properties in engineered systems. Metal Ion Interactions with Apo-Concanavalin A and Some Observations on Metal Ion Requirements and Sugar Binding by Bandeiraea simplicifolia I Lectin.

Israel Journal of Chemistry21 (1), DOI: /ijch Blumberg, S., and Tal, N. Effect of divalent metal ions on the digestibility of concanavalin A by endopeptidases. a reexamination of the kinetics of its interactions with Ca 2+-ions and fluorescent saccharide.

Biochem. Biophys. Kinetic analysis of calcium binding to concanavalin A. Inorg. Bioc – PubMed. The Role of Divalent Metal Ions in Enzymatic DNA Ligation by Mark Robert Taylor A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Biological Chemistry) in the University of Michigan Doctoral Committee: Associate Professor Patrick J.

O'Brien, Chair Professor David R. Engelke. A sulfation‐controlled binding of heavy metal ions to glycans was realized using electrochemical analysis. The artwork presents glassy carbon electrodes modified by a series of hyaluronans with sim. DNA molecules was very dim, so the maximum concentration of divalent ions was no more than 5mmol/L.

Particularly, Mn2+ had the strongest effect on the attenuation of DNA fluorescence intensity among these metal ions.

Even [Mn2+] was as low as 1mmol/L, the fluorescence intensity of DNA was too weak to be observed clearly. Abstract.

Lectins are a diverse group of proteins and glycoproteins that exhibit specific binding for certain carbohydrates. Proteins with this property have been described in a wide variety of taxa, ranging from bacteria (e.g. Neter ) to slime molds (Barondes and Haywood ) and lower vertebrates (Simpson et al.

), but the best characterized examples are from plants.The lectin concanavalin A (ConA) sequentially binds a transition metal ion in the metal-binding site S1 and a calcium ion in the metal-binding site S2 to form its saccharide-binding site.

Metal-free ConA crystals soaked with either Zn 2+ (apoZn-ConA) or Co 2+ (apoCo-ConA) display partial binding of these ions in the proto-transition metal.Biochemistry All Publications/Website.

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