Purification and some properties of cobalamin-dependent methionine synthase from rat liver

Kazuhiro Yamada, Takamasa Tobimatsu, Tetsunori Kawata, Masahiro Wada, Akio Maekawa, Tetsuo Toraya

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5 Citations (Scopus)


Cobalamin-dependent methionine synthase was purified from rat liver. The enzyme activity was separated into two peaks upon Mono-Q column chromatography. Peaks I and II of the enzyme, eluted in this order, were purified 18,000- and 44,000-fold in overall yields of 0.7 and 1.8%, respectively. Peak II methionine synthase, the major fraction, was homogeneous as judged by SDS-polyacrylamide gel electrophoresis. The enzyme was a large monomeric protein with an apparent molecular weight of 143,000 Da. Interconversion of the enzyme between the two peaks was not observed during purification procedures. The enzyme required S-adenosylmethionine and a reducing system for activity. Apparent Km values of the peak II enzyme for 5-methyltetrahydrofolate and homocysteine were 75 and 1.7μM, respectively.

Original languageEnglish
Pages (from-to)177-186
Number of pages10
JournalJournal of Nutritional Science and Vitaminology
Issue number2
Publication statusPublished - 1997


  • 5-methyltetrahydrofolate- homocysteine methyltransferase
  • S-adenosylmethionine
  • cobalamin
  • methionine synthase
  • rat liver

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Nutrition and Dietetics


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