Evaluation of Fluorescence Polarization Method for Binding Study in Carbohydrate-Lectin Interaction.

Oda, Yasuo; Kinoshita, Mitsuhiro; Nakayama, Katsuyoshi; Kakehi, Kazuaki

doi:10.1248/bpb.21.1215

Cited by 19 publications

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“…The times to 40 meq/kg (PV) were determined as the induction period for each stored sample. Synergism was calculated by comparing the induction periods, modifying the equations of Satue-Gracia et al (16) and Alaiz et al (17), [2] where a = antioxidant, p = protein, and c = control. Antioxidant capacity by the ABTS .+ test, fluorescence values, and PV induction times were analyzed by one-way ANOVA to determine the pooled SD.…”

Section: Methodsmentioning

confidence: 99%

“…Although antioxidants have been frequently studied in oils, emulsions, and other foods, there have been few reports of how proteins-which are commonly present in foods-may affect the activity of antioxidants in foods. Most antioxidants of interest for foods have one or more phenolic hydroxyl groups, and several studies have demonstrated that molecules with this structure may bind to proteins (2)(3)(4)(5). Polyphenols may associate with proteins through hydrophobic interactions and hydrogen bonding (2), and a range of phenolic antioxidants also has been shown to bind to bovine skin proteins (3).…”

mentioning

confidence: 99%

“…Most antioxidants of interest for foods have one or more phenolic hydroxyl groups, and several studies have demonstrated that molecules with this structure may bind to proteins (2)(3)(4)(5). Polyphenols may associate with proteins through hydrophobic interactions and hydrogen bonding (2), and a range of phenolic antioxidants also has been shown to bind to bovine skin proteins (3). Red wine antioxidants bind to human lipoproteins and protect them from metal ion-dependent and -independent oxidation (4).…”

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confidence: 99%

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Synergistic effect of BSA on antioxidant activities in model food emulsions

Pablos

Gordon

2004

J Americ Oil Chem Soc

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Sunflower oil-in-water emulsions containing TBHQ, caffeic acid, epigallocatechin gallate (EGCG), or 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox), both with and without BSA, were stored at 50 and 30°C. Oxidation of the oil was monitored by determination of the PV, conjugated diene content, and hexanal formation. Emulsions containing EGCG, caffeic acid, and, to a lesser extent, Trolox were much more stable during storage in the presence of BSA than in its absence even though BSA itself did not provide an antioxidant effect. BSA did not have a synergistic effect on the antioxidant activity of TBHQ. The BSA structure changed, with a considerable loss of fluorescent tryptophan groups during storage of solutions containing BSA and antioxidants, and a BSA-antioxidant adduct with radical-scavenging activity was formed. The highest radicalscavenging activity observed was for the isolated protein from a sample containing EGCG and BSA incubated at 30°C for 10 d. This fraction contained unchanged BSA as well as BSA-antioxidant adduct, but 95.7% of the initial fluorescence had been lost, showing that most of the BSA had been altered. It can be concluded that BSA exerts its synergistic effect with antioxidants because of formation of a protein-antioxidant adduct during storage, which is concentrated at the oil-water interface owing to the surface-active nature of the protein. SCHEME 1a Values with the same superscript letter in each row are not significantly different (P > 0.05). ABTS, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt; for other abbreviations see Table 1.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Synergistic effect of BSA on antioxidant activities in model food emulsions

Pablos

Gordon

2004

J Americ Oil Chem Soc

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“…Therefore, in some cases, we can observe the molecular interaction even between lectin and intact cells. We examined the usefulness and limitation of the FP method in the observation of molecular interaction between plant lectins and polysaccharides and yeast cells (30). Of the lectins examined, Con A, wheat germ agglutinin, Lens curinalis agglutinin, CSL, Pisum sativus agglutinin, Tulipa gesneriana lectin, and Lycoris radiata agglutinin, fluorescein-labeled Con A (estimated molecular mass 100,000 Da) showed obvious FP change upon binding.…”

Section: Applicationsmentioning

confidence: 99%

Fluorescence Polarization: Analysis of Carbohydrate–Protein Interaction

Kakehi

Oda

Kinoshita

2001

Analytical Biochemistry

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“…Because the rate of the enzyme reaction between HA oligomers and hyaluronidase was slow at 47C, we could measure the binding between hyaluronidase and 3-AB HA oligomers at this temperature according to the procedure reported previously [9]. The results using 20 mM concentrations of oligomers are shown in Table 1.…”

Section: Binding Between 3-ab Ha Oligomers and Hyaluronidasementioning

confidence: 99%

Anomalous migration of hyaluronic acid oligomers in capillary electrophoresis: Correlation to susceptibility to hyaluronidase

et al. 2001

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During high-resolution capillary electrophoresis analysis in an electrolyte solution containing a neutral polymer, small oligomers of regularly arranged acidic polysaccharides such as hyaluronic acid and N-acetylneuraminic acid polymers showed reversal of the migration order. This anomalous migration was well correlated with their reported biological activity. In the present study, we analyzed hyaluronidase action on the purified hyaluronic acid oligomers using capillary electrophoresis and found that hydrolytic and transglycosylation actions by hyaluronidase were dependent on the molecular sizes of hyaluronic acid oligomers, and well correlated to their migration profiles. Furthermore, fluorescent polarization technique was employed for understanding the relationship between molecular size of hyaluronic acid oligomers and their electromigrations.

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Evaluation of Fluorescence Polarization Method for Binding Study in Carbohydrate-Lectin Interaction.

Cited by 19 publications

References 0 publications

Synergistic effect of BSA on antioxidant activities in model food emulsions

Synergistic effect of BSA on antioxidant activities in model food emulsions

Fluorescence Polarization: Analysis of Carbohydrate–Protein Interaction

Anomalous migration of hyaluronic acid oligomers in capillary electrophoresis: Correlation to susceptibility to hyaluronidase

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