단백질의 메틸화 : 20여년 연구의 회고

백운기,김상덕 ( Woon Ki Paik,Sang Duk Kim ) 생화학분자생물학회 1991 생화학총설집 Vol.3 No.-

Crotalus adamanteus 의 L - Amino Acid Oxidase 의 열로 인한 불활성에 대한 식초산염의 보호작용 기전

백운기,김상덕 ( Woon Ki Paik,San Gduk Kim ) 생화학분자생물학회 1975 BMB Reports Vol.8 No.3

The mechanism of the protective action of acetate against heat-inactivation of the L-amino acid oxidase (L-amino acid:oxygen oxidoreductase (deaminating, EC 1.4.3.2) of Crotalus adamanteus venom has been investigated. The entropy of activation for the heat-inactivation of the enzyme in the presence of acetate was 224 e.u. compared to 114 e.u. in its absence. The Km value of the enzyme for L-arginine was decreased from 3. 86 mM to 0. 77 mM in the presence of 330mM acetate. The Vmax was reduced from 227 to 161 ㎕O₂ consumed per hour per ㎎ of enzyme protein. These results are taken to mean that the protective action of acetate is by preventing the enzyme protein from assuming a less ordered state, at high pH, by combining at a site different from the substrate-binding site.

일반논문 1 : 김종익의 유언과 경성여자의학전문학교 설립과정

백운기 ( Woon Ki Paik ),김상덕 ( Sang Duk Kim ) 연세대학교 의과대학 의사학과 의학사연구소 2011 연세의사학 Vol.14 No.1

Dr. Rosetta Hall, an American missionary physician, and Dr. Jeong-hee Gil, a young Korean physician, founded the Joseon (Keijo) Women`s Training Institute in 1928. Between 1933 and 1937, Dr. Gil and her husband, Dr. Kim Tak-won, maintained and financed the medical institute. Supporting the institute placed a heavy burden on the young doctors who were just establishing their private medical practice. Despite this burden, they undertook the work necessary to elevate the institute to a full medical college. In order to generate the substantial funds needed to establish the medical college, they created a foundation for the “creation of a women`s medical college” in 1934 and solicited funding. In 1937, a philanthropist interested in furthering education, Mr. Kim Jong-ik, agreed to donate the funding necessary to elevate the institute to a medical college. Mr. Kim, however, unexpectedly contracted dysentery and died. In his will, Mr. Kim bequeathed a portion of his estate to upgrading the institute to a medical college. The executor, contrary to Mr. Kim`s intent as set forth in his will, however, did not use the funds to elevate the institute, but rather established a completely new women`s medial college. The executor`s actions were a clear violation of Drs. Kim`s and Gil`s legal rights as beneficiaries under the will. They, nonetheless, accepted the outcome, because challenging the executor`s actions under Japanese rule would have been futile as Dr. Kim was a noted anti-Japanese patriot well known to the Japanese. Moreover, Sato Gozo had been Dr. Kim`s teacher at the Keijo Medical College. Most importantly, their dream of establishing a women`s medical college in Korea had been realized regardless of how. Regardless of whether the institute had been elevated to a medical college or not, Drs. Kim Tak-won and Gil Jeong-hee made great sacrifices to further the education of women medical doctors in Korea and should be recognized for their great contributions to the creation of Korea Women`s Medical College.

개구리에서 암모니아 독에 대한 Arginine의 해독작용에 관한 연구

홍영숙,백운기,Hong, Young-Sook,Paik, Woon-Ki 생화학분자생물학회 1973 한국생화학회지 Vol.6 No.1

개구리에서 암모니아의 $LD_{99.9}$은 체중 20gm 당(當) 0.65mM 이었다(32.5mM/kg). 백서에서의 $LD_{99.9}$는 이에 비하면 1/3 밖에 아니된다. 그리고 개구리에서 체중 20gm 당 2.0mM의 arginine은 암모니아 $LD_{99.9}$량의 독성을 완전히 해독하였다. 그외 glutamic acid, aspartic acid 그리고 glycine을 주사했을 때는 암모니아 독에 대한 해독작용은 없었고 아마노산 자체의 독성을 나타내었다. The $LD_{99.9}$ of ammonium acetate in frogs was 0.65 mM/20 gm of the body weight. The $LD_{99.9}$ of ammonium acetate in rats when compared with frogs is about one-third of that in frogs, and 2 mM of arginine/20 gm of the body weight completely prevented the toxicity of $LD_{99.9}$ of ammonium acetate in frogs.

개구리에서 암모니아 독에 대한 Arginine 의 해독작용에 관한 연구

홍영숙,백운기 ( Young Sook Hong,Woon Ki Paik ) 생화학분자생물학회 1973 BMB Reports Vol.6 No.1

Th.e LD_(99.9) of ammonium acetate in frogs was 0. 65 mM/20 gm of the body weight. The LD_(99.9) of ammonium acetate in rats when compared with frogs is about one-third of that in frogs, and 2 mM of arginine/20 gm of the body weight completely prevented the toxicity of LD_(99.9) of ammonium acetate in frogs.

Synthesis and Characterization of N-Methylamidinoglycine : an Isomer of Creatine

조영봉,백운기,Young-Bong Cho,R. John Stedman,Woon Ki Paik Korean Chemical Society 1985 대한화학회지 Vol.29 No.4

N-Methylamidinoglycine, an isomer of creatine which was postulated to be formed enzymatically in vitro, has been synthesized by coupling glycine with N, S-dimethylthiopseudouronium iodide in a yield of approxirnately 60%. On heating in acidic solution, it was converted to a cyclized form (isocreatinine) in analogy with the conversion of creatine to creatinine(anhydrous form). Structures were confirmed by an elemental analysis and proton NMR spectroscopy. Further studies on their characteristics were compared with those of creatine and creatinine in regard to isoelectric points(pI), retardation coefficients(Rf) on thin layer chromatography, and elution profiles on amino acid analyzer. In order to facilitate the comparison, $^{14}C$-labeled creatine, creatinine, isocreatine and isocreatinine were also synthesized. 시험관내에서 효소에 의해 생성될 수 있을 것으로 생각되는 N-Methylamidinoglycine(isocreatine)을 glycine과 N, S-dimethylthiopseudouronium iodide로 부터 약 60% 수득율로 합성하였고, isocreation의 산성수용액을 가열하여, creatine이 creatinine으로 탈수 고리화되는 것처럼, 고리화된 isocreatinine도 얻었다. 한편 이들 화합물에 대해 원소분석, nmr 스펙트럼, 박층 크로마토그피(Rf) 및 아미노산분석기에서의 elution rate도 검토하였으며, 등전점을 측정하기 위해서 $^{14}C$-creatine, $^{14}C$-creatinine, $^{14}C$-isocreatine 및 $^{14}C$-isocreatinine도 합성하였다.

Euglena의 Cytochrome C552 Methylation에 관한 연구

이향우(Hyang Woo Lee),백운기(Woon Ki Paik) 대한약학회 1988 약학회지 Vol.32 No.6

Post-translational modification of protein amino acid residues is a well known metabolic phenomenon. One such side chain modification, protein methylation, occur ubiquitously in nature, in organism ranging from prokaryotic to eukaryotic and the biological significance of protein methylation has begun to emerge. The observation that cytochrome C methylation facilitates the binding of this hemoprotein to mitochondria could be placed as the one of the examples along this line. However, the detail biological meaning of cytochrome C methylation is remained to be clarified. In the aspect of such reason this research was done. The results of this experiment were; 1) pure Euglena gracilis cytochrome C552 was isolated, 2) methylarginine and methylmethionine were not found in cytochrome C552 sequence, 3) however, Unknown Peak at 20.78 min of retention time was found, and 4) this Unknown Peak was found only from Euglena cytochrome C552, so far.

Effect of Naturally Occurring Basic Compounds on the Cytochrome C Binding to Mitochondria

박광숙,박인국,전길자,김상덕,백운기,Park, Kwang-Sook,Desi, Suhas,Park, In-Kook,Jun, Gil-Ja,Kim, Sang-Duk,Paik, Woon-Ki Korean Society for Biochemistry and Molecular Biol 1987 한국생화학회지 Vol.20 No.2

미토콘드리아와 Cytochrome c 결합에 미치는 염기성 화합물의 영향

박광숙,Suhas Desi,박인국,전길자,김상덕,백운기 ( Kwang Sook Park,Suhas Desi,In Kook Park,Gil Ja Jun,Sang Duk Kim,Woon Ki Paik ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.2

Binding of horse heart (methyl-^(14)C)cytochrome c reductively methylated with (^(14)C) formaldehyde to isolated rat liver mitochondria has been investigated. The number of binding sites is calculated to be 56 pmoles of cytochrome c/㎎ of mitochondria) protein, and the affinity constant (K_a) to be 1.79 × 107M^(-1). Various naturally occurring basic compounds including histones, protamine and polyamines are highly inhibitory on the (methyl-^(14)C)cytochrome c binding. Almost all of (methyl-^(14)C)cytochrome c bound to mitochondria can be released from the mitochondria by subsequent treatment with nonlabeled cytochrome c. Although histone H3 (arginine-rich histone) has much stronger inhibitory effect on the (methyl-^(14)C)cytochrome c binding than non-labeled cytochrome c at equimolar concentration when present in the binding assay mixture, only a fraction of bound (methyl-^(14)C)cytochrome c can be freed from mitochondria by treatment with histone H3. Evidence indicates that these effect are not merely a consequence of electrostatic influence on the cytochorme c receptor of mitochondria.

Enzymatic Carboxyl-Methylesterification of Myelin Basic Protein

전길자,홍성열,이향우,김명희,김상덕,백운기,Jun, Gil-Ja,Hong, Sung-Ryul,Lee, Hyang-Woo,Kim, Myung-Hee,Tuck, Martin,Kim, Sang-Duk,Paik, Woon-Ki 생화학분자생물학회 1985 한국생화학회지 Vol.18 No.2

소뇌의 myelin 염기성 단백질(MBP 또는 AI 염기성 단백질)이 in vitro에서 S-adenosylmethione:protein carboxyl-O-methyltransferase(protein methylase II; EC 2.1.1.24)에 대한 우수한 기질이였으며 $K_m$ 값은 $4.0{\times}10^{-5}\;M$ 이었다. protein methylase II에 의해 methyl화 된 MBP-[methyl-$^{14}C$]를 pepsin으로 소화시켜 peptide mapping 한 결과 진한 방사성 반점 한개와 흐린 반점이 한개 나타났다. 이 실험 결과 protein methylase II가 MBP에 대해서 비교적 강한 부위 특이성을 나타내고 있음을 알수 있었다. 이 효소는 MBP를 최대로 4.9 mole 퍼센트 methyl화 시킬 수 있다. Jimpy mutant mice의 뇌에 있는 protein methylase II의 양은 이상이 없는 다른 형제들이 가지고 있는 효소량과 차이가 없었다. Bovine brain myelin basic protein (MBP or AI basic protein) was found to serve as an excellent in vitro substrate for S-adenosylmethionine:protein-carboxyl O-methyltransferase (protein methylase II; EC 2.1.1.24) with a $K_m$ value of $4.0{\times}10^{-5}\;M$. Peptide mapping of pepsin-digested [methyl-$^{14}C$]-MBP methylated by purified protein methylase II shows one major and one minor spot on autofiuorography, indicating a relatively strong site-specificity of the enzyme towards MBP. At maximum, the enzyme can methylate 4.9 mole per cent of the MBP. Unlike protein methylase I [EC 2.1.1.23) which methylates arginine residues of MBP, protein methylase II activity in the brains of jimpy mutant mice (one of the dysmyelinating mutants) does not differ from the value of their normal littermates.