An endogenous proteinacious inhibitor for S-adenosyl-L-methionine-dependent transmethylation reactions; identification of S-adenosylhomocystein as an integral part.
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 6.3x10(-6) M towards protein methylase II.
Seo
D W
DW
Department of Pharmacy, College of Pharmacy, SungKyunKwan University, Suwon, Korea.
Han
J W
JW
Hong
S Y
SY
Paik
W K
WK
Lee
H W
HW
D000818:Animals; D002845:Chromatography; D002851:Chromatography, High Pressure Liquid; D004791:Enzyme Inhibitors / Q000302:isolation & purification / Q000494:pharmacology*; D008099:Liver / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D011497:Protein O-Methyltransferase / Q000302:isolation & purification; D012435:S-Adenosylhomocysteine / Q000494:pharmacology*; D012436:S-Adenosylmethionine / Q000502:physiology*; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013552:Swine
D004791:Enzyme Inhibitors; D012436:S-Adenosylmethionine; D012435:S-Adenosylhomocysteine; D011497:Protein O-Methyltransferase