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  • Book
    edited by Jennifer J. Kohler, Steven M. Patrie.
    Contents:
    Introduction to glycosylation and mass spectrometry / Steven M. Patrie, Michael J. Roth, and Jennifer J. Kohler
    PART I ENRICHMENT AND ISOLATION METHODS
    Tandem lectin weak affinity chromatography for glycoprotein enrichment / Zhi Yuan Ma, Yuliya Skorobogatko, and Keith Vosseller
    CSC technology: Selective labeling of glycoproteins by mild oxidation to phenotype cells / Andreas Hofmann, Damaris Bausch-Fluck, and Bernd Wollscheid
    Use of boronic acid nanoparticles in glycoprotein enrichment / Yawei Xu, Lijuan Zhang, and Haojie Lu
    Incorporation of unnatural sugars for the identification of glycoproteins / Balyn W. Zaro, Howard C. Hang, and Matthew R. Pratt
    Characterization of membrane-associated glycoproteins using lectin affinity chromatography and mass spectrometry / Yashu Liu, Jintang He, and David M. Lubman
    Sialic acid capture-and-release and LC-MS(n) analysis of glycopeptides / Jonas Nilsson and Göran Larson
    PART II SAMPLE PREPARATION
    In-solution digestion of glycoproteins for glycopeptide-based mass analysis / Eden P. Go, Kathryn R. Rebecchi, and Heather Desaire
    Nano-HPLC-MS of glycopeptides obtained after nonspecific proteolysis / Gerhild Zauner, Carolien A.M. Koeleman, André M. Deelder, and Manfred Wuhrer
    PART III SEPARATION METHODS
    Glycopeptide enrichment for MALDI-TOF mass spectrometry analysis by hydrophilic interaction liquid chromatography solid phase extraction (HILIC SPE) / Pia Hønnerup Jensen, Simon Mysling, Peter Højrup, and Ole Nørregaard Jensen
    Separation and identification of glycoforms by capillary electrophoresis with electrospray ionization mass spectrometric detection / Alina D. Zamfir, Corina Flangea, Alina Serb, Ana-Maria Zagrean, Andreas M. Rizzi, and Eugen Sisu
    Structural separations by ion mobility-MS for glycomics and glycoproteomics / Larissa S. Fenn and John A. McLean
    PART IV QUANTITATION METHODS
    Quantitative analysis of glycoprotein glycans / Ron Orlando
    Stable isotope labeling of N-glycosylated peptides by enzymatic deglycosylation for mass spectrometry-based glycoproteomics / Hiroyuki Kaji and Toshiaki Isobe
    Approaches for site mapping and quantification of o-linked glycopeptides / Peng Zhao, Stephanie H. Stalnaker, and Lance Wells
    Glycan profiling: Label-free analysis of glycoproteins / Yoshinao Wada
    PART V COMPUTATIONAL TOOLS
    Introduction to informatics in glycoprotein analysis / Kiyoko F. Aoki-Kinoshita
    Software tools for glycan profiling / Chuan-Yih Yu, Anoop Mayampurath, and Haixu Tang
    PART VI CASE STUDIES IN MASS SPECTROMETRY OF GLYCOPROTEINS
    Quantitative characterization of glycoproteins in neurodegenerative disorders using iTRAQ / Min Shi, Hyejin Hwang, and Jing Zhang
    Quantitative proteomic analysis of N-linked glycoproteins in human tear fluid / Lei Zhou and Roger W. Beuerman
    Elucidation of N-glycosites within human plasma glycoproteins for cancer biomarker discovery / Penelope Drake, Birgit Schilling, Brad Gibson, and Susan Fisher
    Characterizing the glycosylation state of therapeutic recombinant glycoproteins. / Nicole Samuels, David Kates, Jun Liu, and Joanne Severs.
    Digital Access Springer 2013
  • Article
    Webb D, Thadepalli H, Bach V.
    Rev Infect Dis. 1979 Jan-Feb;1(1):170-4.
    Of 22 patients who were suspected of having bacterial endocarditis and who were treated with cefoxitin intravenously (8-12 g per day), 12 were evaluated for responses to therapy. Ten patients had infections due to a single pathogen, and two had polymicrobial infections. Staphylococci were isolated from eight patients, and streptococci from four; both of these pathogens were susceptible to 2-16 micrograms of cefoxitin/ml. Staphylococcus aureus and four strains of anaerobic bacteria, including Bacteroides fragilis (minimal inhibitory concentration, 32 micrograms/ml), were isolated from one patient. The average level of cefoxitin in serum was 32.8 micrograms/ml (range, 14.5-64 micrograms/ml) at 1 hr after an intravenous dose of 2 g; after 5 hr the average level in serum was 8.5 micrograms/ml (range, 2-20 micrograms/ml). The mean (+/- SD) level of cefoxitin in myocardial tissues from eight rabbits at 1 hr following a 250-mg/kg dose of the antibiotic was 4 +/- 0.5 micrograms/g. On the average, patients were treated for 29 days (range, 14-40 days), and they became afebrile in 6.2 days (range, three to 20 days). Both clinical and microbiologic responses to cefoxitin therapy were excellent in 10 patients with monobacterial infections. Both patients with polymicrobial infections were not cured. One, who was infected with a mixed flora of anaerobes, died; the other was cured after surgical valvectomy. These results suggest that cefoxitin is effective in the treatment of endocarditis due to a single susceptible organism but that this antibiotic should be used with caution in patients whose endocarditis is caused by a mixed population of bacterial pathogens.
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