Isolation and properties of an S-adenosyl-L-methionine binding protein from the green alga, Chlamydomonas reinhardi

Y. Nakano, N. Koizumi, T. Kusano, H. Sano

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    A protein that binds S-adenosyl-L-methionine (AdoMet) was isolated by successive chromatography from vegetative cells of Chlamydomonas reinhardi. The relative molecular masses of native and denatured proteins were calculated to be 15 kDa and 16 kDa, respectively. The reaction was specific to AdoMet and reversible as shown by competition experiments. The optimal pH for binding ranged between 7.5 and 9.0, and the apparent Ka for AdoMet was 1.0 μmol/L. Results suggested that the protein may function as the carrier to stabilize AdoMet, which is otherwise labile in the cellular environment.

    Original languageEnglish
    Pages (from-to)707-711
    Number of pages5
    JournalJournal of Plant Physiology
    Volume157
    Issue number6
    DOIs
    Publication statusPublished - 2000

    Keywords

    • Chlamydomonas reinhardi
    • S-adenosyl-L-methionine

    ASJC Scopus subject areas

    • Physiology
    • Agronomy and Crop Science
    • Plant Science

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