Purification and properties of tauropine dehydrogenase from a red alga, Rhodoglossum japonicum

Minoru Sato, Masaaki Takeuchi, Nobuhiro Kanno, Eizou Nagahisa, Yoshikazu Sato

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)


    Tauropine dehydrogenase which is a member of 'opine' dehydrogenases and catalyzes the reductive condensation of taurine with pyruvate was purified from a red alga, Rhodoglossum japonicum using a combination of ammonium sulfate fractionation, gel filtration, affinity, and ion exchange chromatography. The molecular mass of this enzyme, obtained by HPLC using TSK SW2000G in its native form and SDS-PAGE in its denatured form, was 39000 and 42000, respectively. This means tauropine dehydrogenase has monomeric structure like other opine dehydrogenases. The relative activities for amino acids as substrate were 100 for taurine, 17 for valine and 12 for homotaurine. The apparent Km values for taurine, pyruvate and NADH were 15.0 mM, 0.80 mM and 0.04 mM, and for tauropine and NAD+ were 30 mM and 0.12 mM, respectively. Diurnal change of tauropine content was observed in R. japonicum, tauropine increased in the daytime and decreased in the nighttime.

    Original languageEnglish
    Pages (from-to)673-678
    Number of pages6
    Issue number1
    Publication statusPublished - 1993 Jun 1


    • D-rhodoic acid
    • Rhodoglossum japonicum
    • opine
    • purification
    • seaweed
    • tauropine dehydrogenase

    ASJC Scopus subject areas

    • Aquatic Science


    Dive into the research topics of 'Purification and properties of tauropine dehydrogenase from a red alga, Rhodoglossum japonicum'. Together they form a unique fingerprint.

    Cite this