An endogenous proteinacious inhibitor for S-adenosyl-L-methionine-dependent transmethylation reactions; Identification of S-adenosylhomocysteine as an integral part

Authors
Seo, DW Han, JW Hong, SY Paik, WK Lee, HW
Citation
Dw. Seo et al., An endogenous proteinacious inhibitor for S-adenosyl-L-methionine-dependent transmethylation reactions; Identification of S-adenosylhomocysteine as an integral part, ARCH PH RES, 22(3), 1999, pp. 237-242
Citations number
15
Categorie Soggetti
Pharmacology & Toxicology
Journal title
ARCHIVES OF PHARMACAL RESEARCH
ISSN journal
02536269 → ACNP
Volume
22
Issue
3
Year of publication
1999
Pages
237 - 242
Database
ISI
SICI code
0253-6269(199906)22:3<237:AEPIFS>2.0.ZU;2-R
Abstract
A proteinacious inhibitor with a molecular weight of 1,600 Da which inhibit s S-adenosyl-L-methionine-dependent transmethylation reactions was purified from porcine liver to homogeneity by procedures including boiling, Sephade x G-25 column chromatography and repeated HPLC. Employing both Nuclear Magn etic Resonance (NMR) and Fast Atom Bombardmet-Mass (FAB-Mass) spectroscopy, S-adenosylhomocysteine was conclusively identified as an integral part of the inhibitor. The purified S-adenosylhomocysteine was competitive with S-a denosyl-L-methionine with Ki value of 6.3x10(-6) M towards protein methylas e II.