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Search: WFRF:(Ohlson Sten) > (2000-2004)

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1.
  • Bergström, Maria, et al. (author)
  • Lectin affinity capillary electrophoresis in glycoform analysis applying the partial filling technique
  • 2004
  • In: Journal of chromatography. B. - : Elsevier BV. - 1570-0232 .- 1873-376X. ; 809:2, s. 323-329
  • Journal article (peer-reviewed)abstract
    • The study of protein glycosylation and its significance in biological interactions is a field of growing interest. This work demonstrates a lectin-based separation of protein glycoforms of α1-acid glycoprotein (AGP or orosomucoid) with capillary electrophoresis. Glycoform analysis was performed with a "partial filling technique" with the lectin Concanavalin A (Con A) as affinity ligand. Con A separated human AGP into two peaks, the first peak included AGP glycoforms without biantennary glycans, and the second peak represented the fraction that had one or more biantennary glycans. The applicability of the method was demonstrated with the analysis of AGP from clinical samples and AGP treated with N-glycosidase F. The AGP separation was also used as a reporter system to estimate the dissociation constant (KD) between Con A and a competing sugar. © 2004 Elsevier B.V. All rights reserved.
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  • Liljeblad, Mathias, et al. (author)
  • A Lectin Immunosensor Technique for Determination of α1-Acid Glycoprotein Fucosylation
  • 2001
  • In: Analytical Biochemistry. - : Elsevier BV. - 0003-2697 .- 1096-0309. ; 288:2, s. 216-224
  • Journal article (peer-reviewed)abstract
    • The fucosylation of α1-acid glycoprotein (AGP), an acute-phase protein, is known to change in association with inflammatory diseases. Thus, fucosylation of AGP could be a potential diagnostic or prognostic marker. The change in fucosylation has previously been investigated using crossed affinoimmunoelectrophoresis, high-pH anion-exchange chromatography, and lectin ELISA. This study describes a surface plasmon resonance-based affinity biosensor assay for quantification of the fucosylation of AGP. Diluted EDTA plasma or serum was injected directly in a BIACORE 2000 biosensor. AGP was captured on the sensor surface using immobilized antibodies and a fucose-binding lectin from Aleuria aurentia was then used for the detection of fucosylation. The feature of the biosensor makes it possible to determine both the amount of bound AGP and the amount of bound lectin. Using a calibration curve it was possible to obtain a fucosylation ratio that was independent of AGP concentration. The assay was validated against a lectin ELISA and used to follow inflammation in patients with severe burns.
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  • Result 1-15 of 15

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