An Endogenous Proteinacious Inhibitor for S-Adenosyl-L-methionine-dependent Transmethylation Reactions; Identification of S-Adenosylhomocysteine as an Integral Part

  • Seo, Dong-Wan (Department of Pharmacy, College of Pharmacy, SungkyunKwan University) ;
  • Han, Jeung-Whan (Department of Pharmacy, College of Pharmacy, SungkyunKwan University) ;
  • Hong, Sung-Youl (Department of Genetic Engineering, College of Life Science and Natural Resources Sungkyunkwan University) ;
  • Paik , Woon-Ki (Department of Biochemistry, School of Medicine, Ajou University) ;
  • Lee, Hyang-Woo (Department of Pharmacy, College of Pharmacy, SungkyunKwan University)
  • Published : 1999.06.01

Abstract

A proteinacious inhibitor with a molecular weight of 1,600 Da which inhibits S-adenosyl-L-methionine-dependent transmethylation reactions was purified from porcine liver to homogeneity by procedures including boiling, Sephadex G-25 column chromatography and repeated HPLC. Employing both Nuclear Magnetic Resonance (NMR) and Fast Atom Bombardment-Mass (FAB-Mass) spectroscopy, S-adenosylhomocysteine was conclusively identified as an integral part of the inhibitor. The purified S-adenosylhomocysteine was competitive with S-adenosyl-L-methionine with Ki value of $6.3{\times}10^{-6}$ M towards protein methylase II.

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