An endogenous proteinacious inhibitor forS-adenosyl-L-methionine-dependent transmethylation reactions; Identification ofS-adenosylhomocysteine as an integral part
1999
Sŏ, Tong-wan | Han, Jeung Whan | Hong, Sung Youl | Paik, Woon Ki | Lee, Hyang Woo
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 6.3×10⁻⁶ M towards protein methylase II.
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