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  • 1.Tandem in space (空間性串聯) 2.Tandem in time (時間性串聯)

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    api-3696530
    26 vizualizări14 pagini
    Tandem mass spectrometry can be used to analyze post-translational modifications through either tandem in space or tandem in time techniques. It allows identification of phosphorylated positions on proteins and analysis of protein glycosylation, such as characterization of N-linked and O-linked oligosaccharide cores and glycoforms. Liquid chromatography, enzymatic digestion, and mass spectrometry methods can provide detailed information on glycans and glycoforms.

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    Tandem mass spectrometry can be used to analyze post-translational modifications through either tandem in space or tandem in time techniques. It allows identification of phosphorylated positions on proteins and analysis of protein glycosylation, such as characterization of N-linked and O-linked oligosaccharide cores and glycoforms. Liquid chromatography, enzymatic digestion, and mass spectrometry methods can provide detailed information on glycans and glycoforms.

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    Attribution Non-Commercial (BY-NC)
    Descărcați ca PDF, TXT sau citiți online pe Scribd
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    26 vizualizări14 pagini

    1.Tandem in space (空間性串聯) 2.Tandem in time (時間性串聯)

    Încărcat de

    api-3696530
    Tandem mass spectrometry can be used to analyze post-translational modifications through either tandem in space or tandem in time techniques. It allows identification of phosphorylated positions on proteins and analysis of protein glycosylation, such as characterization of N-linked and O-linked oligosaccharide cores and glycoforms. Liquid chromatography, enzymatic digestion, and mass spectrometry methods can provide detailed information on glycans and glycoforms.

    Drepturi de autor:

    Attribution Non-Commercial (BY-NC)
    Descărcați ca PDF, TXT sau citiți online pe Scribd
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    din 14

    Tandem mass spectrometry

    Mass spectrometry for analyses of


    Post-translational modification
    1.Tandem in space (空間性串聯)
    2.Tandem in time (時間性串聯)

    LID
    TOF-TOF

    Ion Trap Ion Trap


    Radio frequency field is scanned
    multiple collision-induced dissociation

    1
    Protein Phosphorylation

    Parent ion scan


    (Precursor ion scan)

    2
    Analysis of phosphorylated positions

    3
    Protein glycosylation

    4
    5
    Glycoproteins

    glycoform

    6
    N-linked oligosaccharide core
    Enzyme release

    Oligomannose-type N-linked oligosaccharides


    Hybrid and complex native N-linked oligosaccharides

    O-linked oligosaccharide core O-linked oligosaccharide core


    Hydrazine release

    7
    Functions of glycoproteins

    C3 convertase

    Methods for analyses of glycan

    bind to C8 and C9

    Analyses of glycan by liquid chromatography

    8
    N-linked oligosaccharide core O-linked oligosaccharide core

    N-glycosidase F

    2-AB labeling
    HPLC

    1. Normal phase HPLC (NP)


    Glucose uint (dextran)

    2. Reverse phase HPLC (RP)


    Arabinose unit

    3. Weak Anionic Exchanger (WAX)

    1. Normal phase HPLC (NP)


    Glucose uint (dextran)
    2. Reverse phase HPLC (RP)
    Arabinose unit
    3. Weak Anionic Exchanger (WAX)

    9
    1. Normal phase HPLC (NP)
    Glucose uint (dextran)
    2. Reverse phase HPLC (RP)
    Arabinose unit
    3. Weak Anionic Exchanger (WAX)

    Enzyme array

    2D electrophoresis and MALDI-TOF MS

    10
    Glycoform ?

    MALDI-TOF and glycoform


    MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight)

    N-glycosidase F

    11
    Ion Trap

    Tandem mass spectrometry (MSn)

    Ion Trap

    12
    Chemical modification

    13
    14

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