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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 11 (1972), S. 4692-4695 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 35 (1993), S. 90-92 
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; α1-acid glycoprotein ; Complex glycans ; Allergic reaction ; Terfenadine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Little is known about the alterations that have occurred at the individual glycosylation sites in allergy patients or how these glycosylation patterns may change after anti-allergy treatments. Using reverse-phase HPLC, we have quantitated the glycoforms present at the individual glycosylation sites on orosomucoid isolated from the sera of allergic reaction patients and an allergic reaction patient treated with the antihistamine Terfenadine. The glycan structures isolated from the five glycosylation sites for the individual taking Terfenadine were all within normal ranges. It is suggested that if the changes in glycosylation in OMD in the allergic state are functionally driven, then it should be possible to correlate biological activities with quantitative changes at the individual glycosylation sites, and hence further define the role of OMD in allergy and inflammation.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 31 (1991), S. 63-66 
    ISSN: 1612-1112
    Keywords: Orosomucoid ; Phthalates ; ±1 glycoprotein ; Cigarettes ; Lipocalin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Cigarette smokers have a phthalate noncovalently bound to their serum orosomucoid. The phthalate, whose concentration is dependent on the number of cigarettes smoked, is tentatively identified as a metabolite of di-(2-ethylhexyl)-phthalate, a common plasticizer. The binding of the ligand is in concert with the membership of orosomucoid in the lipocalin family and its role as a transporter of basic drugs. Smoking may have an effect on drug pharmacokinetics that is difficult to predict.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 31 (1991), S. 478-480 
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Orosomucoid ; Complex glycans ; α1 glycoprotein ; Glycopeptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The glycoforms contained within each glycosylation site of orosomucoid can be separated by reverse-phase HPLC without removal of the associated peptide or chemical derivatization. The chromatographic properties of the glycopeptides are dominated by the peptide portion but modified by the hydrophilicity of the glycan in a regular manner depending on its size. Assignments for known structures are readily made, permitting quantitative assessment of changes in glycoform concentration at individual glycosylation sites.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 37 (1993), S. 144-148 
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Orosomucoid ; Complex glycans ; α1-acid glycoprotein ; Individual glycosylation sites
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The glycosylation patterns of multiglycosylated proteins reflect both the cellular control of glycosyl transferase activity and the local control of the transfer event. Little information is available concerning these mechanisms. Changes in glycosylation occur in the disease state and provide a convenient way of examining the control mechanism(s) operating at individual glycosylation sites. Chromatographic methods have been applied to the human orosomucoid (OMD) isolated from seventeen different pathologies. Based on the distribution of the glycans at the individual sites it is clear that the major protein-glycan interactions that restrict glycosylation in “normal” OMD remain intact in the disease state in the presence of changing glycosyl transferase activity.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Orosomucoid ; α1-acid glycoprotein ; Lipocalin ; Monoclonal antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The accessibility of the surface of human orosomucoid to monoclonal antibodies (MAbs) was investigated by size-exclusion HPLC to examine the validity of its proposed membership in the lipocalin family. The N-terminus half of the molecule contains all the five glycan chains, and of fifty-six MAbs, only one bound to this piece of the polypeptide backbone, indicating that extensive screening was taking place. The simultaneous binding properties of selected MAbs to the fully glycosylated molecule was examined by size exclusion HPLC. The pattern of inhibition was contiguous, with all regions being overlapped. The epitopes of four MAbs having mutual noncompetitive binding were found to be appropriately spaced when placed on a preliminary three dimensional model of orosomucoid. Together, the results support a structure for orosomucoid composed of an exposed continuous protein surface, and a glycan surface screening the remaining protein. Such a structure is provided by the antiparallel β-barrel motif of the lipocalins.
    Type of Medium: Electronic Resource
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