Showing 1 - 6 results of 6 for search '"matrix-assisted laser desorption/ionization"', query time: 0.07s Refine Results
  1. 1

    High-performance liquid chromatography analysis of ganglioside carbohydrates at the picomole level after ceramide glycanase digestion and fluorescent labeling with 2-aminobenzamide... by Wing, DR, Garner, B, Hunnam, V, Reinkensmeier, G, Andersson, U, Harvey, D, Dwek, R, Platt, F, Butters, T

    Published 2001
    “…Glycan structures were confirmed by exoglycosidase digestion and/or matrix-assisted laser desorption/ionization mass spectrometry.…”
    Journal article
  2. 2

    Controlled glycosylation of therapeutic antibodies in plants. by Tekoah, Y, Ko, K, Koprowski, H, Harvey, D, Wormald, M, Dwek, R, Rudd, P

    Published 2004
    “…Gel release of glycans and detection by high-performance liquid chromatography (HPLC), together with computer assisted analysis and matrix-assisted laser desorption/ionization time-of-flight (MALD-TOF) mass spectrometry, revealed that the plant-derived anti-rabies mAb with KDEL contained mainly oligomannose type N-glycans while the plant-derived anti-colorectal cancer mAb carried mainly biantennary glycans with and without a pentose sugar, that is thought to be xylose. …”
    Journal article
  3. 3

    Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway. by Crispin, M, Harvey, D, Chang, V, Yu, C, Aricescu, A, Jones, E, Davis, S, Dwek, R, Rudd, P

    Published 2006
    “…A mammalian N-acetylglucosamine (GlcNAc) transferase I (GnT I)-independent fucosylation pathway is revealed by the use of matrix-assisted laser desorption/ionization (MALDI) and negative-ion nano-electrospray ionization (ESI) mass spectrometry of N-linked glycans from natively folded recombinant glycoproteins, expressed in both human embryonic kidney (HEK) 293S and Chinese hamster ovary (CHO) Lec3.2.8.1 cells deficient in GnT I activity. …”
    Journal article
  4. 4

    Use of the α-mannosidase I inhibitor kifunensine allows the crystallization of apo CTLA-4 homodimer produced in long-term cultures of Chinese hamster ovary cells by Yu, C, Crispin, M, Sonnen, A, Harvey, D, Chang, V, Evans, E, Scanlan, C, Stuart, D, Gilbert, R, Davis, S

    Published 2011
    “…It is shown that the α-mannosidase I inhibitor kifunensine, which has previously been used for the purpose of glycoprotein crystallization in short-term (3-5 d) cultures, is apparently stable enough to be used to produce highly endoglycosidase H-sensitive glycoprotein in long-term (3-4 week) cultures of stably transfected Chinese hamster ovary (CHO) cells. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry-based analysis of the extracellular region of the cytotoxic T-lymphocyte antigen 4 (CTLA-4; CD152) homodimer expressed in long-term CHO cell cultures in the presence of kifunensine revealed that the inhibitor restricted CTLA-4 glycan processing to Man9GlcNAc2 and Man5GlcNAc2 structures. …”
    Journal article
  5. 5

    Comparison of the N-linked glycans from soluble and GPI-anchored CD59 expressed in CHO cells. by Wheeler, S, Rudd, P, Davis, S, Dwek, R, Harvey, D

    Published 2002
    “…Exoglycosidase digestions and analysis by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry were used to define the relative amounts of the bi-, tri-, and tetraantennary glycans and to investigate the distribution of N-acetyllactosamine extensions between their antennae. …”
    Journal article
  6. 6

    Cellular effects of deoxynojirimycin analogues: inhibition of N-linked oligosaccharide processing and generation of free glucosylated oligosaccharides. by Mellor, H, Neville, D, Harvey, D, Platt, F, Dwek, R, Butters, T

    Published 2004
    “…When these FOS structures (>30, including >20 species not present in control cells) were characterized by enzyme digests and MALDI-TOF (matrix-assisted laser-desorption ionization-time-of-flight) MS, all were found to be polymannose-type oligosaccharides, of which the majority were glucosylated and had only one reducing terminal GlcNAc (N-acetylglucosamine) residue (FOS-GlcNAc1), demonstrating a cytosolic location. …”
    Journal article