First experience with the use of the Pharmacia PhastSystem for the characterization of haemoglobins by isoelectric focusing

Kramlová, M.; Přistoupil, T.I.; Fričová, V.; Kraml, J

doi:10.1016/s0021-9673(00)94868-4

Cited by 15 publications

(11 citation statements)

References 4 publications

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“…Isoelectric Focusing. Isoelectric focusing of the β-LG-ALGO conjugate was performed by using the Pharmacia-Phast System (Kramlova et al, 1986). The protein bands were detected by staining with Coomassie Brilliant Blue.…”

Section: Methodsmentioning

confidence: 99%

Functional Improvement of β-Lactoglobulin by Conjugating with Alginate Lyase-Lysate

Hattori

Oginö

Nakai

et al. 1997

J. Agric. Food Chem.

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Bovine β-lactoglobulin−alginic acid oligosaccharide (β-LG−ALGO) conjugate was prepared by the Maillard reaction to improve the function of β-LG. The molar ratio of β-LG to ALGO in the conjugates was 1:7. The isoelectric point of the conjugate was 4.55, which is lower than that of β-LG. Fluorescence studies suggested that the conformation around Trp had changed in the conjugate and that the surface of the conjugate was covered with saccharide chain. Structural analyses with monoclonal antibodies indicated that the conformation around Val15−Ile29 (β-sheet) in the conjugate had changed, while native structure was maintained around Thr125−Lys135 (α-helix). By conjugation with ALGO, β-LG was endowed with high heat stability. The emulsifying activity and the aggregating property of β-LG was improved in the conjugate. Keywords: β-Lactoglobulin; alginic acid; alginate lyase; neoglycoconjugate; functional improvement; acidic polysaccharide; protein conjugation; emulsification; solubility; retinol-binding; lipocalin

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Section: Methodsmentioning

confidence: 99%

Functional Improvement of β-Lactoglobulin by Conjugating with Alginate Lyase-Lysate

Hattori

Oginö

Nakai

et al. 1997

J. Agric. Food Chem.

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“…Isoelectric Focusing. The isoelectric point of each β-LG-CMD conjugate was determined by isoelectric focusing with the Pharmacia Phast System (Kramlova et al, 1986). The electrophoresed protein bands were detected by staining with Coomassie Brilliant Blue.…”

Section: Methodsmentioning

confidence: 99%

Role of the Polysaccharide Content and Net Charge on the Emulsifying Properties of β-Lactoglobulin−Carboxymethyldextran Conjugates

Nagasawa

Ohgata

Takahashi

et al. 1996

J. Agric. Food Chem.

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β-Lactoglobulin (β-LG)−carboxymethyldextran (CMD) conjugates were prepared by using water-soluble carbodiimide. Three kinds of CMD differing in molecular mass (40, 70, and 162 kDa) were used to investigate the effects of different CMD contents and net charge on the functional changes in β-LG. The emulsifying properties of these β-LG−CMD conjugates were investigated under various conditions by evaluating the stability of oil/water emulsions prepared with oleic acid and the β-LG−CMD conjugates. The emulsifying ability of β-LG was greatly improved by conjugating with CMD in the acidic pH range in the presence of less than 0.5 M NaCl. After heating at 80 °C for 10 min, the emulsifying stability of the β-LG−CMD conjugates was higher than that of β-LG. It is thought that increasing the polysaccharide content and shifting the isoelectric point of β-LG to the acidic side by conjugating with CMD of a high molecular weight would be effective in improving the emulsifying properties of β-LG under unfavorable conditions. Keywords: β-Lactoglobulin; neoglycoconjugate; functional improvement; acidic polysaccharide; protein conjugation; emulsification; lipocalin

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“…Isoelectric focusing of the ␤-LG-ALG conjugates was performed by using the Pharmacia-Phast System (Kramlova et al, 1986). The electrophoresed protein bands were detected by staining with Coomassie Brilliant Blue.…”

Section: Isoelectric Focusingmentioning

confidence: 99%

Functional Improvement of Alginic Acid by Conjugating with β‐Lactoglobulin

Hattori

Aiba

Nagasawa

et al. 1996

Journal of Food Science

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Two bovine ␤-lactoglobulin-alginic acid (␤-LG-ALG) conjugates were prepared to improve the function of ALG by using water-soluble carbodiimide and the Maillard reaction. Fluorescence studies suggested that the conformation around Trp had been changed in each conjugate and that the surface of each conjugate was covered with polysaccharide chain. Structural analyses with monoclonal antibodies indicated that the conformation around 15Val-29IIe (␤-sheet) in each conjugate had changed, while the native structure was maintained around 125Thr-135Lys (␣-helix). After conjugating with ␤-LG, ALG showed retinolbinding and high emulsifying ability. The aggregating property of ALG in acid and in the presence of Ca 2+ was improved in each conjugate.

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First experience with the use of the Pharmacia PhastSystem for the characterization of haemoglobins by isoelectric focusing

Cited by 15 publications

References 4 publications

Functional Improvement of β-Lactoglobulin by Conjugating with Alginate Lyase-Lysate

Functional Improvement of β-Lactoglobulin by Conjugating with Alginate Lyase-Lysate

Role of the Polysaccharide Content and Net Charge on the Emulsifying Properties of β-Lactoglobulin−Carboxymethyldextran Conjugates

Functional Improvement of Alginic Acid by Conjugating with β‐Lactoglobulin

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