Two-step purification of human α1-acid glycoprotein

Succari, M; Foglietti, Marie-José; Percheron, F

doi:10.1016/s0378-4347(00)84061-x

Cited by 10 publications

(1 citation statement)

References 15 publications

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“…AGP was purified from EDTA plasma using a modified two-step ion-exchange chromatography method (13). Briefly, 2 ml plasma was dialyzed against 20 mM citrate-phosphate buffer, pH 4.0, and centrifuged.…”

Section: Methodsmentioning

confidence: 99%

A Lectin Immunosensor Technique for Determination of α1-Acid Glycoprotein Fucosylation

Liljeblad

Rydén

Ohlson³

et al. 2001

Analytical Biochemistry

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Section: Methodsmentioning

confidence: 99%

A Lectin Immunosensor Technique for Determination of α1-Acid Glycoprotein Fucosylation

Liljeblad

Rydén

Ohlson³

et al. 2001

Analytical Biochemistry

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Alpha‐1‐Acid Glycoprotein Concentration and the Protein Binding of Disopyramide in Healthy Subjects

Kishino

Nomura

et al. 1995

The Journal of Clinical Pharma

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Age- and gender-related changes in serum alpha 1-acid glycoprotein (AAG) concentration and the serum protein binding of disopyramide were examined after intensive medical examination. Based on the clinical chemistry tests over 51 points, 245 subjects were diagnosed as healthy and 71 subjects (22.5%) revealed an abnormal value for at least one item. In the healthy subjects, serum AAG concentration in men was significantly higher than in women (men, 0.78 +/- 0.18 mg/mL, mean +/- SD; women, 0.67 +/- 0.16 mg/mL). In contrast, there were no significant differences in the AAG concentration between age groups for men and women and in the unbound fraction of disopyramide. Gender changes AAG concentration. Age, however, does not change AAG concentration and the protein binding of the basic drug.

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Modulation of human polymorphonuclear neutrophil functions by ?1acid glycoprotein

et al. 1990

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alpha 1-Acid glycoprotein (alpha 1-AGP), a naturally occurring human plasma protein and acute-phase reactant, was extracted by a two-step procedure from sera collected from four healthy men. Its activity was tested in vitro on human polymorphonuclear (PMN) functions (migration, aggregation, O2- generation). alpha 1-AGP was not chemoattractant but inhibited the PMN response to the chemoattractant formylmethionyl-leucyl-phenylalanine without affecting spontaneous migration (Boyden and agarose methods of assessment). At concentrations between 0.15 and 0.45 mg/ml, alpha 1-AGP exerted an aggregating effect with a maximal effective concentration of 0.3 mg/ml. alpha 1-AGP inhibited superoxide generation by PMNs stimulated either by opsonized zymosan or phorbol myristate acetate. This inhibition varied according to the intensity of the stimulation. At low stimulus concentrations, a dose-dependent inhibition of membrane-associated PMN responsiveness to soluble or particulate stimuli was observed. These findings suggest that alpha 1-AGP may be able to prevent PMN activation in the course of inflammatory processes in vivo.

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Two-step purification of human α1-acid glycoprotein

Cited by 10 publications

References 15 publications

A Lectin Immunosensor Technique for Determination of α1-Acid Glycoprotein Fucosylation

A Lectin Immunosensor Technique for Determination of α1-Acid Glycoprotein Fucosylation

Alpha‐1‐Acid Glycoprotein Concentration and the Protein Binding of Disopyramide in Healthy Subjects

Modulation of human polymorphonuclear neutrophil functions by ?1acid glycoprotein

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