High-performance liquid chromatography determination of α1-acid glycoprotein in small volumes of plasma from neonates

Stumpe, Michael; Miller, Cynthia J.; Morton, Neil S.; Bell, Graham; Watson, David

doi:10.1016/j.jchromb.2005.11.039

Cited by 22 publications

(26 citation statements)

References 20 publications

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“…The acid precipitation of AGP from serum or aqueous samples was performed according to a previously-reported procedure [20]. In this pretreatment method, a 65 μL portion of serum and 130 μL of 0.5 M perchloric acid were combined and vortexed for 20 s (Note: Use appropriate chemical hazard precautions when handling perchloric acid) [35].…”

Section: Methodsmentioning

confidence: 99%

“…A number of schemes have been developed to isolate AGP from serum and related samples prior to the analysis of this glycoprotein by liquid chromatography or CE [12,13,18–20]. Previous methods for the purification of AGP have often involved multiple chromatographic steps (e.g., ion-exchange and dye-ligand affinity chromatography), which can be time-consuming and generally require relatively large sample volumes (e.g., 1–2 mL of serum or plasma) [18,19].…”

Section: Introductionmentioning

confidence: 99%

“…Previous methods for the purification of AGP have often involved multiple chromatographic steps (e.g., ion-exchange and dye-ligand affinity chromatography), which can be time-consuming and generally require relatively large sample volumes (e.g., 1–2 mL of serum or plasma) [18,19]. A method based on acidic precipitation has been described for the isolation of AGP from 50 μL of plasma [20]. However, significant interferences in the resulting samples have still been noted with this approach, which has resulted in the further use of anti-AGP antibodies in columns or on magnetic beads to purify AGP [12,13].…”

Section: Introductionmentioning

confidence: 99%

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Glycoform analysis of alpha1-acid glycoprotein based on capillary electrophoresis and electrophoretic injection

Zhang

Clarke

et al. 2017

Journal of Chromatography A

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A method based on capillary electrophoresis (CE) with electrophoretic injection and absorbance detection was developed for the direct analysis of AGP glycoforms in human serum. Electrophoretic injection of AGP was performed in the reversed-polarity mode of CE with a capillary coated with poly(ethylene oxide) and that had minimal electroosmotic flow. This situation created an essentially stationary interface between the sample and running buffer during injection and sample stacking. This approach allowed an 11,000-fold increase in sample loading for a 5 min injection versus hydrodynamic injection and without introducing any significant levels of extra band-broadening. This method was used with sample pretreatment methods based on acid precipitation and desalting to examine AGP glycoforms in only 65 μL of serum. A limit of detection of 2.1–11.3 nM was obtained for the major AGP glycoform bands in serum, and the sample pretreatment method gave a recovery of 72.3–80.9% for these glycoforms. The precision for the migration times was ± 0.08–0.13% and the precision for the peak areas was ± 0.34–1.18% when using serum samples and an internal standard. This method was used for both normal pooled serum and serum from individuals with systemic lupus erythematosus. Results were obtained in a separation time of 25 min and allowed the comparison of up to eleven glycoform bands in these samples. A similar approach may be useful in examining additional glycoproteins in serum or other types of biological samples.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Glycoform analysis of alpha1-acid glycoprotein based on capillary electrophoresis and electrophoretic injection

Zhang

Clarke

et al. 2017

Journal of Chromatography A

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“…Recently, high-performance liquid chromatography (HPLC) has been widely applied as a method for the determination of aromatic component groups (Kishino and Miyazaki, 2004;Sun et al, 2006;Stumpe et al, 2006); however, it is not clear if HPLC can be applicable for the determination of the target glycoprotein from jellyfish oral-arms. In this study, an HPLC method was developed to determine both the quality and quantity of the target glycoprotein from jellyfish oral-arms, and an optimum extraction method for TGPs was selected by utilizing the HPLC method.…”

Section: Introductionmentioning

confidence: 99%

Screening of extraction methods for glycoproteins from jellyfish (Rhopilema esculentum) oral-arms by high performance liquid chromatography

Ren

Zhao

et al. 2009

J. Ocean Univ. China

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In order to select an optimum extraction method for the target glycoprotein (TGP) from jellyfish (Rhopilema esculentum) oral-arms, a high performance liquid chromatography (HPLC)-assay for the determination of the TGP was developed. Purified target glycoprotein was taken as a standard glycoprotein. The results showed that the calibration curves for peak area plotted against concentration for TGP were linear (r = 0.9984, y = 4.5895x+47.601) over concentrations ranging from 50 to 400 mgL -1 . The mean extraction recovery was 97.84% (CV2.60%). The fractions containing TGP were isolated from jellyfish (R. esculentum) oral-arms by four extraction methods: 1) water extraction (WE), 2) phosphate buffer solution (PBS) extraction (PE), 3) ultrasound-assisted water extraction (UA-WE), 4) ultrasound-assisted PBS extraction (UA-PE). The lyophilized extract was dissolved in Milli-Q water and analyzed directly on a short TSK-GEL G4000PWXL (7.8 mm×300 mm) column. Our results indicated that the UA-PE method was the optimum extraction method selected by HPLC.

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“…The lower limits of quantitation for parent drug and metabolite were 1 and 2 ng/mL, respectively. Plasma concentrations of a 1 -acid glycoprotein were determined according to a previously published method (23).…”

Section: Methodsmentioning

confidence: 99%

Pharmacokinetic Investigation of Imatinib Using Accelerator Mass Spectrometry in Patients with Chronic Myeloid Leukemia

Boddy¹,

Sludden²,

Griffin³

et al. 2007

Clinical Cancer Research

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Purpose:To investigate the potential use of accelerator mass spectrometry (AMS) in the study of the clinical pharmacology of imatinib. Experimental Design: Six patients who were receiving imatinib (400 mg/d) as part of their ongoing treatment for chronic myeloid leukemia (CML) received a dose containing a trace quantity (13.6 kBq) of 14 C-imatinib. Blood samples were collected from patients before and at various times up to 72 h after administration of the test dose and were processed to provide samples of plasma and peripheral blood lymphocytes (PBL). Samples were analyzed by AMS, with chromatographic separation of parent compound from metabolites. In addition, plasma samples were analyzed by liquid chromatography/mass spectrometry (LCMS). Results: Analysis of the AMS data indicated that imatinib was rapidly absorbed and could be detected in plasma up to 72 h after administration. Imatinib was also detectable in PBL at 24 h after administration of the 14 C-labeled dose. Comparison of plasma concentrations determined by AMS with those derived by LCMS analysis gave similar average estimates of area under plasma concentration time curve (26 F 3 versus 27 F 11 Ag/mLÁh), but with some variation within each individual. Conclusions: Using this technique, data were obtained in a small number of patients on the pharmacokinetics of a single dose of imatinib in the context of chronic dosing, which could shed light on possible pharmacologic causes of resistance to imatinib in CML.

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High-performance liquid chromatography determination of α1-acid glycoprotein in small volumes of plasma from neonates

Cited by 22 publications

References 20 publications

Glycoform analysis of alpha1-acid glycoprotein based on capillary electrophoresis and electrophoretic injection

Glycoform analysis of alpha1-acid glycoprotein based on capillary electrophoresis and electrophoretic injection

Screening of extraction methods for glycoproteins from jellyfish (Rhopilema esculentum) oral-arms by high performance liquid chromatography

Pharmacokinetic Investigation of Imatinib Using Accelerator Mass Spectrometry in Patients with Chronic Myeloid Leukemia

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