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Probe Mass Spectrometry (probe + mass_spectrometry)

Distribution by Scientific Domains
Chemistry100%

Kinds of Probe Mass Spectrometry

  • radical probe mass spectrometry
    		•

    Selected Abstracts

    Ability of N -acetylcarnosine to protect lens crystallins from oxidation and oxidative damage by radical probe mass spectrometry (RP-MS)

    RAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 19 2010
    Ji-won Ha
    The application of Radical Probe Mass Spectrometry based on protein footprinting studies is described to investigate the effectiveness of the antioxidant N -acetylcarnosine (NAC) in preventing oxidative damage to lens crystallins present in the eye of mammals. Despite separate clinical trials which have reported the benefit of administering NAC to the eye as a 1% topical solution for the treatment of human cataract, no evidence was found to suggest that the antioxidant had any significant direct effect on reducing the levels of oxidation within the most abundant lens crystallins, , and ,-crystallin, at the molecular level at increasing concentrations of NAC. The results of this laboratory study suggest that the therapeutic benefit demonstrated in clinical trials is associated with the nature or formulation of the topical solution and/or that the mode of action of NAC as an antioxidant is not a direct one. Copyright © 2010 John Wiley & Sons, Ltd. [source]

    Detection and structural features of the ,B2-B3-crystallin heterodimer by radical probe mass spectrometry (RP-MS)

    JOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 5 2009
    Hélène Diemer
    Abstract The predilection of the ,-crystallin B2 subunit to interact with the ,B3 subunit rather than self associate is evident by the detection of the ,B2-B3-crystallin heterodimer by native gel electrophoresis and electrospray ionisation time-of-flight (ESI-TOF) mass spectrometry under non denaturing conditions. The complex has been detected for the first time and its molecular mass is measured to be 47 450 ± 1 Da. Radical probe mass spectrometry (RP-MS) was subsequently applied to investigate the nature of the heterodimer through the limited oxidation of the subunits in the complex. Two peptide segments of the ,B2 subunit and six of the ,B3 subunit were found to oxidise, with far greater oxidation observed within the ,B3 versus the ,B2 subunit. This, and the observation that the oxidation data of ,B2 subunit is inconsistent with the structure of the ,B2 monomer, demonstrates that the protection of ,B2 is conferred by its association with ,B3 subunit within the heterodimer where only the residues of, and towards, its N -terminal domain remain exposed to solvent. The results suggest that the ,B2 subunit adopts a more compacted form than in its monomeric form in order for much of its structure to be enveloped by the ,B3 subunit within the heterodimer. Copyright © 2009 John Wiley & Sons, Ltd. [source]

    Ability of N -acetylcarnosine to protect lens crystallins from oxidation and oxidative damage by radical probe mass spectrometry (RP-MS)

    RAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 19 2010
    Ji-won Ha
    The application of Radical Probe Mass Spectrometry based on protein footprinting studies is described to investigate the effectiveness of the antioxidant N -acetylcarnosine (NAC) in preventing oxidative damage to lens crystallins present in the eye of mammals. Despite separate clinical trials which have reported the benefit of administering NAC to the eye as a 1% topical solution for the treatment of human cataract, no evidence was found to suggest that the antioxidant had any significant direct effect on reducing the levels of oxidation within the most abundant lens crystallins, , and ,-crystallin, at the molecular level at increasing concentrations of NAC. The results of this laboratory study suggest that the therapeutic benefit demonstrated in clinical trials is associated with the nature or formulation of the topical solution and/or that the mode of action of NAC as an antioxidant is not a direct one. Copyright © 2010 John Wiley & Sons, Ltd. [source]