Regulation of spinach-leaf nitrate reductase by reversible phosphorylation

    Research output: Contribution to journalComment/debate

    109 Citations (Scopus)

    Abstract

    Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.

    Original languageEnglish
    Pages (from-to)121-126
    Number of pages6
    JournalBiochimica et Biophysica Acta. Molecular Cell Research
    Volume1137
    Issue number1
    DOIs
    Publication statusPublished - 1992

    Cite this

    @article{b46059a1b1f4428b809ee5b0b7df58af,
    title = "Regulation of spinach-leaf nitrate reductase by reversible phosphorylation",
    abstract = "Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.",
    author = "Carol MacKintosh",
    year = "1992",
    doi = "10.1016/0167-4889(92)90109-O",
    language = "English",
    volume = "1137",
    pages = "121--126",
    journal = "Biochimica et Biophysica Acta. Molecular Cell Research",
    issn = "0167-4889",
    publisher = "Elsevier",
    number = "1",

    }

    Regulation of spinach-leaf nitrate reductase by reversible phosphorylation. / MacKintosh, Carol.

    In: Biochimica et Biophysica Acta. Molecular Cell Research, Vol. 1137, No. 1, 1992, p. 121-126.

    Research output: Contribution to journalComment/debate

    TY - JOUR

    T1 - Regulation of spinach-leaf nitrate reductase by reversible phosphorylation

    AU - MacKintosh, Carol

    PY - 1992

    Y1 - 1992

    N2 - Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.

    AB - Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.

    U2 - 10.1016/0167-4889(92)90109-O

    DO - 10.1016/0167-4889(92)90109-O

    M3 - Comment/debate

    VL - 1137

    SP - 121

    EP - 126

    JO - Biochimica et Biophysica Acta. Molecular Cell Research

    JF - Biochimica et Biophysica Acta. Molecular Cell Research

    SN - 0167-4889

    IS - 1

    ER -