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  • 1
    ISSN: 1573-4986
    Keywords: glycoprotein ; glycosylation ; gp120 ; HIV ; MALDI-TOF-MS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Neutral complex-type N-glycans of the envelope glycoprotein 120 of HIV-2, propagated in different host cells, display cell-type specific variations. In order to identify typical structural elements, glycans were analysed by gel filtration, by enzymic sequencing and, in part, by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The characteristic substituents of di- tri- and tetraantennary carbohydrate units thus observed include N-acetyllactosamine repeats, bisecting N-acetylglucosamine and fucose linked to the chitobiose core as well as to N-acetyllactosamine antennae. Each glycoprotein preparation displayed a characteristic set of glycoforms. Abbreviations: endo H, endo-β-N-acetylglucosaminidase H; E-PHA, Phaseolus vulgaris agglutinin E4; GlcNAcOH, N-acetyl-glucosaminitol; gp120/HUT78(MOLT4/Mφ/PBL/U937), external envelope glycoprotein 120 of HIV-2, strain D194, propagated in HUT78 (MOLT4, Mφ, PBL, U937) cells; gu, glucose units; HPAEC, high-pH anion-exchange chromatography; MALDI-TOF-MS, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; Mφ, human monocytes/macrophages; PBL, human peripheral blood lymphocytes; PNGase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F
    Type of Medium: Electronic Resource
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