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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.
Protein methylase 2 에 의한 Myelin 염기성 단백질의 Carboxyl - methylesterification
전길자,홍성열,이향우,김명희,Martin Tuck,김상덕,백운기 ( Gil Ja Jun,Sung Ryul Hong,Hyang Woo Lee,Myung Hee Kim,Martin Tuck,Sang Duk Kim,Woon Ki Paik ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.2
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 0-methyltransferase (protein methylase II; EC 2.1.1.24) with a K_m value of 4.0×10^(-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 autofluorography, 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.
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.