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Post-translational modifications in the nuclear region of young, aged, and cataract human lenses.

Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. Research Abstract Details 

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  • Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. Abstract Text:

    peter g hainsPeter G Hains,roger j w truscottRoger J W Truscott,peter g hainsPeter G Hains,roger j w truscottRoger J W Truscott,

    The urea-soluble proteins from the nucleus of two young, two aged, and two early-stage nuclear cataract lenses were subjected to tryptic digestion and analysis by 2D LC-MS/MS. Several novel post-translational modifications were identified. Deamidation was, by far, the most common modification. A number of differences were found in cataract compared to normal lenses, most notably an increase in the number of oxidized tryptophan residues. Semiquantitative analysis revealed that there appeared to be a trend toward increased levels of deamidation with age; however, there was no apparent increase upon the onset of nuclear cataract. This is in contrast to Trp oxidation, where an increase in the extent of modification was apparent in cataract lenses when compared to aged normal lenses. These findings suggest Trp oxidation may be involved in nuclear cataract development.

    Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. Publishing Authors By Initials

    pg hainsPG Hains,rj truscottRJ Truscott,pg hainsPG Hains,rj truscottRJ Truscott,

    For similar investigative techniques: chemistry, analytical: mass spectrometry: tandem mass spectrometry research abstracts see: investigative techniques: chemistry, analytical: mass spectrometry: tandem mass spectrometry research

    PUBMED ID PMID:

    MEDLINE DATE:

    Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Journal of proteome research

    VOLUME: 6

    Page Numbers: 3935-43

    Journal Abbreviation: J. Proteome Res.

    ISSN: 1535-3893

    DAY: 7

    MONTH: 09

    YEAR: 2007

    Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 101128775

    Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. Keywords Mesh Terms:

    KEYWORDS: Tandem Mass Spectrometry

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. Information

    Substance Name: Crystallins

    Registry Number: 0

    Grant and Affiliation Information for Post-translational modifications in the nuclear region of young, aged, and cataract human lenses.

    AFFILIATION: Save Sight Institute, University of Sydney, Sydney, NSW, 2001, Australia.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NEI

    GRANT: R01EY013570-03

    ACRONYM: EY

    MEDLINETA: J Proteome Res

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Post-translational modifications in the nuclear region of young, aged, and cataract human lenses Related Publications

     

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