The affinity of concanavalin A and Lens culinaris hemagglutinin for glycopeptides

Young, N. Martin; Leon, Myron A.

doi:10.1016/0005-2795(74)90015-4

Cited by 44 publications

(11 citation statements)

References 31 publications

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“…The binding affinity of Con A to transferrin was found to be K d = 650 nm. The binding affinity of Con A to transferrin in solution was reported to be 1–2 μM [120], and a value of K d = 1.2 mM was found in SPR experiments of transferrin binding to Con A immobilized on a lectin chip[121]. The binding affinity of Con A to glycoprotein depends upon the glycan structure and multivalent interactions.…”

Section: Resultsmentioning

confidence: 99%

Square-wave voltammetry assays for glycoproteins on nanoporous gold

Pandey

Bhattarai

Pornsuriyasak

et al. 2014

Journal of Electroanalytical Chemistry

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Electrochemical enzyme-linked lectinsorbent assays (ELLA) were developed using nanoporous gold (NPG) as a solid support for protein immobilization and as an electrode for the electrochemical determination of the product of the reaction between alkaline phosphatase (ALP) and p-aminophenyl phosphate (p-APP), which is p-aminophenol (p-AP). Glycoproteins or concanavalin A (Con A) and ALP conjugates were covalently immobilized onto lipoic acid self-assembled monolayers on NPG. The binding of Con A – ALP (or soybean agglutinin – ALP) conjugate to glycoproteins covalently immobilized on NPG and subsequent incubation with p-APP substrate was found to result in square-wave voltammograms whose peak difference current varied with the identity of the glycoprotein. NPG presenting covalently bound glycoproteins was used as the basis for a competitive electrochemical assay for glycoproteins in solution (transferrin and IgG). A kinetic ELLA based on steric hindrance of the enzyme-substrate reaction and hence reduced enzymatic reaction rate after glycoprotein binding is demonstrated using immobilized Con A–ALP conjugates. Using the immobilized Con A-ALP conjugate, the binding affinity of immunoglobulin G (IgG) was found to be 105 nM, and that for transferrin was found to be 650 nM. Minimal interference was observed in the presence of 5 mg mL−1 BSA as a model serum protein in both the kinetic and competitive ELLA. Inhibition studies were performed with methyl D-mannoside for the binding of TSF and IgG to Con A-ALP; IC50 values were found to be 90 μM and 286 μM, respectively. Surface coverages of proteins were estimated using solution depletion and the BCA protein concentration assay.

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Section: Resultsmentioning

confidence: 99%

Square-wave voltammetry assays for glycoproteins on nanoporous gold

Pandey

Bhattarai

Pornsuriyasak

et al. 2014

Journal of Electroanalytical Chemistry

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“…Con A shows the greatest affinity to D-mannose residues in glycoconjugates (Goldstein and So, 1965; and a somewhat lower affinity to Nacetylglucosamine residues (Young and Leon, 1974;Krusius et al, 1976;Kornfeld and Ferris, 1975;Baenziger and Fiete, 1979). Con A also binds with high &inity to the photoreceptor molecule of the rods, rhodopsin (Steinemann and Stryer, 1973).…”

Section: Scleramentioning

confidence: 99%

Lectin binding to the human retina

Söderström

1988

Anat. Rec.

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Formalin-fixed, paraffin-embedded tissue sections of the human retina were stained with different fluorescein isothiocyanate-conjugated lectins. The lectins used were concanavalin A (Con A), Triticum vulgaris (WGA), glycine maximum (SBA), Dolichos biflorus (DBA), Ulex europaeus (UEA I), Arachis hypogaea (PNA), and Ricinus communis (RCA I). Con A stained both the inner and outer segments of the rods and cones, whereas WGA stained the inner and outer segments of the rods and the outer segments of the cones. PNA selectively stained only the inner segments of the cones. In addition, Con A and WGA stained neuron cytoplasm and nerve fibers in different layers of the retina. The results obtained differ in some important aspects from those previously obtained in the frog and monkey retina; this finding may be due to species differences. The results of lectin staining in the normal human retina may form the basis for future studies of retinal diseases.

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“…The binding of ConA Ricinus communis agglutinin and wheat germ agglutinin to human WM membranes was inhibited by monosaccharides specific for each of these lectins, whereas Lens culinaris phytohemagglutinin had common inhibitory monosaccharides with ConA and WGA. However, even though LcH discriminates between simple sugars less efficiently than for example ConA, it has turned out to be effective in its discrimination between certain glycopeptides (Young and Leon, 1974). LcH appears to recognise an N-acetylglucosaminylmannobiose structure, while ConA seems to react with a mannobiosyl-N-acetylglucosamine unit (Toyoshima et al, 1972, Young andLeon, 1974).…”

Section: Discussionmentioning

confidence: 99%

“…However, even though LcH discriminates between simple sugars less efficiently than for example ConA, it has turned out to be effective in its discrimination between certain glycopeptides (Young and Leon, 1974). LcH appears to recognise an N-acetylglucosaminylmannobiose structure, while ConA seems to react with a mannobiosyl-N-acetylglucosamine unit (Toyoshima et al, 1972, Young andLeon, 1974).…”

Section: Discussionmentioning

confidence: 99%

Lectin‐Reactive Components in White Matter Membranes from Normal and Multiple Sclerosis Brains

Hukkanen

1982

Journal of Neurochemistry

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Polypeptides derived from human white matter membranes reacted with the radioiodinated lectins concanavalin A, Lens culinaris phytohemagglutinin, Ricinus communis agglutinin and wheat germ agglutinin after electrophoresis in polyacrylamide pore gradient gels. The molecular weights of these lectin-reactive bands were estimated by comparison with radioiodinated protein standards by using the linear relationship between log of the molecular weight and log of the gel concentration reached by the protein after electrophoresis in a polyacrylamide gradient gel. The molecular weight estimates for components reactive with concanavalin A were 176,800, 141,200, 72,800, 52,800, 44,700, 40,000, 24,800 and 23,900. The molecular weights of the bands reactive with both wheat germ agglutinin and Lens culinaris phytohemagglutinin were 138,000, 113,500, 92,100, 52,800, 44,700, 24,800 and 23,900. Wheat germ agglutinin was bound also to a band with a molecular weight of 72,800. Ricinus communis agglutinin bound to bands with estimated molecular weights of 138,000, 72,800, 52,800, 44,700, 24,800 and 23,900. The electrophoretic pattern of lectin-reactive polypeptides derived from normal-appearing white matter of multiple sclerosis brains was not qualitatively different from the lectin-binding pattern of control brain membrane polypeptides.

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The affinity of concanavalin A and Lens culinaris hemagglutinin for glycopeptides

Cited by 44 publications

References 31 publications

Square-wave voltammetry assays for glycoproteins on nanoporous gold

Square-wave voltammetry assays for glycoproteins on nanoporous gold

Lectin binding to the human retina

Lectin‐Reactive Components in White Matter Membranes from Normal and Multiple Sclerosis Brains

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