Langmuir Aggregation of Eosin-Y in Protein and its Application

2002 ◽  
Vol 55 (12) ◽  
pp. 767 ◽  
Author(s):  
Hong-Wen Gao ◽  
Jian-Fu Zhao
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Concanavalin A ◽  
Bovine Serum ◽  
Quantitative Detection ◽  
Eosin Y ◽  
Isothermal Adsorption ◽  
Adsorption Reaction ◽  
Binding Ratio ◽  
Langmuir Aggregation

The microsurface adsorption–spectral correction (MSASC) technique is described and applied to the investigation of the interaction of eosin-Y (EOY) with proteins at pH 3.8. The microelectrostatic fields in proteins cause the aggregation of EOY and it obeys Langmuir isothermal adsorption. Results have shown that the binding ratio of EOY to bovine serum albumin (BSA), ovalbumin (OVA), concanavalin A (ConA), and human γ-globulin (γ-G) are 77 : 1, 23 : 1, 4 : 1, and 83 : 1, the adsorption constants of the complexes were calculated to be 2.82×106, 1.70×105, 1.80×105, and 2.49×104 M–1, and their molar absorptivities 3.20×106, 1.21×106, 1.35×105, and 5.27×106 L mol–1 cm–1 at 540�nm. The adsorption reaction has been applied to the quantitative detection of proteins in samples with satisfactory results.

scholarly journals Effect of Aqueous Extract of Giant Horsetail (Equisetum giganteum L.) in Antigen-Induced Arthritis

2013 ◽  
Vol 7 (1) ◽  
pp. 129-133 ◽  
Author(s):  
Mirian Farinon ◽  
Priscila Schmidt Lora ◽  
Leandro Nicolodi Francescato ◽  
Valquiria Linck Bassani ◽  
AmÉlia Teresinha Henriques ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Extract ◽  
Concanavalin A ◽  
Bovine Serum ◽  
Lymphocyte Proliferation ◽  
Acute Inflammation ◽  
First Time ◽  
B And T Lymphocytes

Equisetum giganteum is a plant used in traditional medicine as diuretic. From our knowledge this is the first time this plant is tested in an in vivo model of acute inflammation. To evaluate the effect of aqueous extract of giant horsetail (AEGH) as immunomodulatory therapy, antigen-induced arthritis (AIA) was generated in mice with methylated bovine serum albumin (mBSA). Inflammation was evaluated by articular nociception, leukocytes migration and lymphocyte proliferation. AEGH reduced nociception at 3, 6 and 24 h (P < 0.01), decreased leukocyte migration (P < 0.015), and inhibited lymphocyte proliferation stimulated with Concanavalin A and Lipopolysaccharide (P < 0.05). In conclusion, AEGH has an anti-inflammatory potential in acute model of inflammation, as well as immunomodulatory effect on both B and T lymphocytes, with an action independent of cytotoxicity.

scholarly journals The binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios

1974 ◽  
Vol 137 (3) ◽  
pp. 575-578 ◽  
Author(s):  
Geoffrey Allen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Dodecyl Sulphate ◽  
Bovine Serum ◽  
Equilibrium Dialysis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Weight Ratio ◽  
Binding Ratio ◽  
High Binding

The extent of binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios was investigated by gel filtration. The weight ratio of bound sodium dodecyl sulphate to bovine serum albumin increases with the NaCl concentration, and, except at low salt concentrations, with the concentration of sodium dodecyl sulphate. In the presence of 1.0g of sodium dodecyl sulphate/l, the binding ratio varied from 1.0 (at 0.04m-Na+) to 2.2 (at 0.44m-Na+). In the presence of 0.24m-Na+, the binding ratio increased with sodium dodecyl sulphate concentration, from 0.9 (0.2g of sodium dodecyl sulphate/l) to 2.0 (5g of sodium dodecyl sulphate/l), at 26°C, in a dilute sodium phosphate buffer. No significant dependence of the binding ratio upon temperature in the range 26–45°C was observed. These results differ from those of Reynolds & Tanford (1970a) obtained by equilibrium dialysis.

Effects of bovine serum albumin on the interaction of concanavalin A and succinyl-concanavalin A with phospholipid bilayers

1985 ◽  
Vol 63 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Christina A. Chicken ◽  
Frances J. Sharom
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Concanavalin A ◽  
High Purity ◽  
Binding Sites ◽  
Bovine Serum ◽  
Lectin Binding ◽  
Affinity Column ◽  
Binding Studies ◽  
High Affinity

Under physiological conditions, concanavalin A interacts with the surface of phospholipid liposomes through two distinct classes of binding sites, a relatively small number of high affinity sites and a much larger number of lower affinity sites. Addition of bovine serum albumin induces extensive additional binding of concanavalin A to liposomal membranes and this binding is saturable and "specific" (α-methyl mannoside inhibitable). Fraction V and high purity albumin both induce almost identical levels of concanavalin A binding to liposomes. Scatchard plots of the binding data demonstrate the induction of a large number of new, relatively high affinity lectin-binding sites on addition of albumin. Albumin-induced binding of concanavalin A to the bilayer surface shows a broad pH optimum and is not inhibited by 40% (w/v) ethylene glycol, suggesting that hydrophobic forces are relatively unimportant. In contrast, divalent succinyl-concanavalin A shows very little tendency to bind to liposomes, either in the absence or presence of albumin. Passage of high purity albumin down a concanavalin A affinity column or treatment with periodate completely eliminates the additional lectin binding. It thus seems likely that albumin-induced concanavalin A binding to liposomes is related to the presence of a concanavalin-A-binding component. This phenomenon may have important implications for lectin-binding studies carried out on membranes which have been exposed to serum proteins.

Investigation on the pH-dependent binding of Eosin Y and bovine serum albumin by spectral methods

2007 ◽  
Vol 127 (2) ◽  
pp. 515-522 ◽  
Author(s):  
Dejiang Gao ◽  
Yuan Tian ◽  
Fanghui Liang ◽  
Danhong Jin ◽  
Yanhua Chen ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Spectral Methods ◽  
Bovine Serum ◽  
Eosin Y ◽  
Ph Dependent

Study on the interaction of bovine serum albumin with acid cyanine 5R and its application in analysis

2006 ◽  
Vol 84 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Fei Lu ◽  
Jing-Hao Pan ◽  
Yun Liu ◽  
Hongfen Zhang ◽  
Yujing Guo ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Peak Potential ◽  
Buffer Solution ◽  
Solution Ph ◽  
Peak Current ◽  
Binding Ratio ◽  
Relative Standard

A supramolecular complex of bovine serum albumin (BSA) with acid cyanine 5R (AC 5R, C.I. acid blue 113, C.I.: 26360) has been shown to form in Tris–HCl buffer solution (pH 7.42) by linear sweep voltammetry (LSV), fluorimetry, and spectrophotometry. The binding ratio and binding constant of BSA with AC 5R have been detected by LSV and fluorimetry. The binding mechanism is also preliminarily discussed. In Tris–HCl buffer solution (pH 7.42), AC 5R can easily be reduced on the mercury electrode, and it has a well-defined LSV peak current (Ip) and peak potential (Ep) at –0.65 V (vs. SCE). In the presence of BSA, the Ipof AC 5R decreases, and the peak potential (Ep) shifts to a more positive potential. The decrease of the second-order derivative of reductive peak current (ΔIp") of AC 5R is proportional to the logarithm of BSA concentration in the range of 1.54 × 10–8mol·L–1– 1.54 × 10–5mol·L–1(r = 0.9931 – 0.9977). The limit of detection of BSA is 9.0 × 10–9mol·L–1. The relative standard deviation is 1.83% (n = 10), and the standard recovery is 97.5%–104.8%. This method can be used to determine BSA concentration on the basis of the interaction of BSA with AC 5R.Key words: bovine serum albumin (BSA), acid cyanine 5R (AC 5R), supramolecule, binding ratio, binding constant, fluorimetry, spectrophotometry, electroanalytical method.

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