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

Dong Wan Seo; Jeung Whan Han; Sung Youl Hong; Woon Ki Paik; Hyang Woo Lee

doi:10.1007/BF02976356

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

Dong Wan Seo, Jeung Whan Han, Sung Youl Hong, Woon Ki Paik, Hyang Woo Lee

Department of Pharmacy

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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 6.3×10^-6 M towards protein methylase II.

Original language	English
Pages (from-to)	237-242
Number of pages	6
Journal	Archives of Pharmacal Research
Volume	22
Issue number	3
DOIs	https://doi.org/10.1007/BF02976356
State	Published - Jun 1999

Keywords

Methylation
Proteinacious inhibitor
S-adenosylhomocysteine

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10.1007/BF02976356

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title = "An endogenous proteinacious inhibitor for S-adenosyl-L-methionine-dependent transmethylation reactions; identification of S-adenosylhomocysteine as an integral part",

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 6.3×10-6 M towards protein methylase II.",

keywords = "Methylation, Proteinacious inhibitor, S-adenosylhomocysteine",

author = "Seo, \{Dong Wan\} and Han, \{Jeung Whan\} and Hong, \{Sung Youl\} and Paik, \{Woon Ki\} and Lee, \{Hyang Woo\}",

year = "1999",

month = jun,

doi = "10.1007/BF02976356",

language = "English",

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journal = "Archives of Pharmacal Research",

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T1 - An endogenous proteinacious inhibitor for S-adenosyl-L-methionine-dependent transmethylation reactions; identification of S-adenosylhomocysteine as an integral part

AU - Seo, Dong Wan

AU - Han, Jeung Whan

AU - Hong, Sung Youl

AU - Paik, Woon Ki

AU - Lee, Hyang Woo

PY - 1999/6

Y1 - 1999/6

N2 - 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.

AB - 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.

KW - Methylation

KW - Proteinacious inhibitor

KW - S-adenosylhomocysteine

UR - https://www.scopus.com/pages/publications/0033146585

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DO - 10.1007/BF02976356

M3 - Article

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SN - 0253-6269

VL - 22

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JO - Archives of Pharmacal Research

JF - Archives of Pharmacal Research

IS - 3

ER -

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

Abstract

Keywords

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