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소의 갑상선에 있는 크산친 옥시다아제에 관한 연구 : [제2보] 효소의 조성과 특성 [Part 2] Composition and Some Properties
이효사 한국농화학회 1978 Applied Biological Chemistry (Appl Biol Chem) Vol.21 No.3
Xanthine oxidase from bovine thyroid glands was found to contain FAD, molybdenum and iron in a ratio 1:0. 36:1. 6. The molecular weight of the thyroid enzyme was similar to that of the milk enzyme when estimated by gel filtration and polyacrylamide gel electrophoresis. The optimum pH for the enzyme activity was 7.8. The pH of the isoelectric point was determined to be 6.2 by electrofacusing. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis experiment indicated that the enzyme was dissociated into subunits and that the molecular weight for the smallest subunit was 65,000 daltons. Absorption spectra were dissimilar between milk and thyroid xanthine oxidase.
소의 갑상선에 있는 크산친 옥시다아제에 관한 연구 : [제1보] 효소의 정제와 기질특이성 [Part 1] Purification and Substrate Specificity
이효사 한국농화학회 1978 Applied Biological Chemistry (Appl Biol Chem) Vol.21 No.2
Xanthine oxidase from bovine thyroid glands was purified to apparent homogeneity when judged by analytical disc gel electrophoresis. The purification procedures include pancreatin digestion, butanol extraction, ammonium sulfate precipitation, calcium phosphate gel adsorption, ultrafiltration, calcium phosphate gel-cellulose column chromatography, gel filtration, preparative Sephadex G-25 column electrophoresis, and preparative polyacrylamide gel electrophoresis. The enzyme was enriched 1, 000-fold. However, its specific activity was markedly low as compared with highly purified milk enzyme. Thyroidal xanthine oxidase exhibited a low specificity for substrates and electron acceptors. The. kinetic properties of thyroid xanthine oxidase were found to be similar to those of the milk enzyme on the basis of Michaelis constants for common substrates.
분리된 흰쥐 간 핵속의 핵단백질의 인산화반응에 미치는 싸이클릭 뉴클레오티드와 인슐린의 영향
이효사,David M . Gibson ( Hyo Sa Lee ) 생화학분자생물학회 1981 BMB Reports Vol.14 No.1
The effects of cyclic nucleotides and insulin on the phosphorylation patterns of nuclear proteins were investigated by SDS polyacrylamide gel electrophoresis analysis following incubation of livar nuclei isolated from normal fed rats with (γ-^(32)P] ATP. Both c-AMP and c-GMP increased markedly the phosphorylation levels of nucleoplasmic proteins with molecular weights above 53,000 daltons while little change was observed with insulin. The effect of c-GMP was much greater than that of c-AMP. On the other hand, cyclic nucleotides and insulin somewhat inhibited rather phosphorylation of nuclear proteins tightly bound to chromatin such as histones and phenol soluble non-histone proteins.
이효사,Lee, Hyo-Sa,Gibson, David M. 생화학분자생물학회 1981 한국생화학회지 Vol.14 No.1
핵단백질의 인산화반응에 미치는 cyclic 뉴클레오티드와 인슐린의 효과를 추구하기 위하여 $[{\gamma}-^{32}P]$ ATP로 정상 흰쥐 간에서 분리한 핵과 incubate한 뒤에 SDS-polyarcy-lamide gel 전기영동을 하여 분석하였다. c-AMP와 c-GMP는 분자량 약 53,000 dalton의 핵단백질의 인산화반응을 심히 증가시키는 반면에, 인슐린은 변동을 거의 주지 않았다. c-GMP의 효과가 c-AMP의 효과보다 더 컸었다. 반면에 cyclic 뉴클레오티드와 인슐린은 histone과 같이 chromatin과 강하게 결합하고 있는 핵단백질과 페놀 용해성 비 histone단백질의 인산화반응은 오히려 어느정도 억제시켰다. The effects of cyclic nucleotides and insulin on the phosphorylation patterns of nuclear proteins were investigated by SDS polyacrylamide gel electrophoresis analysis following incubation of liver nuclei isolated from normal fed rats with $[{\gamma}-^{32}P]$ ATP. Both c-AMP and c-GMP increased markedly the phosphorylation levels of nucleoplasmic proteins with molecular weights above 53,000 daltons while little change was observed with insulin. The effect of c-GMP was much greater than that of c-AMP. On the other hand, cyclic nucleotides and insulin somewhat inhibited rather phosphorylation of nuclear proteins tightly bound to chromatin such as histones and phenol soluble non-histone proteins.
The interaction of rabbit adrenal norepinephrine N - methyl tranferase isozymes with substrates
이효사 생화학분자생물학회 1985 BMB Reports Vol.12 No.4
Norepinephrine N-methyl transferase (NMT) is the enzyme which catalyzes the N-methylation of norepinephrine (NE) to form epinephrine (Epi). The enzyme is present in the cytosol fraction of animal adrenal medulla and S-adenosyl methionine (SAM) is required as the methyl donor. The presence of multiple forms of NMT in adrenal medulla has been indicated by starch gel electrophoresis. Recently, multiple form of NMT have been identified by disc gel electrophoresis and purified to electrophoretically homogenity using hydroxylapitite in our labotatory. The results of the purification indicate that the distribution of NMT isozymes for young rabbits differs from. that observed with adult rabbits. Also our previous experiment has shown that NMT isozymes have a characteristic kinetic behavior with respect to substrate inhibition. Therefore, the work reported here was undertaken to characterize NMT isozymes further in terms of kinetic properties and to isozymes in terms of substrate inhibition.
단식 , 재합식(再合食) 및 인슈린 투여 후에 쥐의 간으로부터 분리된 세포핵의 핵단백질 인산화
이효사,데이비드엠깁슨 한국농화학회 1980 Applied Biological Chemistry (Appl Biol Chem) Vol.23 No.1
Labelling of chromatin proteins with 2P was observed after incubating isolated liver nuclei with [γ-32P] ATP for 5 minutes at 37℃. The pattern of labelling with 32P was examined on SDS polyacrylamide gel electrophoresis with nuclei from rats maintained in a starvation state for 48 hours, following refeeding for 12 hours; and from fed streptozotocin-diabetic rats with insulin injection 6 hours before sacrifice. With 48h starved rat liver nuclei the level of phosphorylation for 0.14M NaCl soluble proteins was decreased in the molecular weights between 41,000 and 200,000 dalrons relative to normal controls. Refeeding the starved rats reversed the change of phosphorylation pattern over 12 hour. The level of phosphorylation for five phenol soluble nonhistone proteins with molecular weights above 59,000 daltons was somewhat decreased with 48h starved rat liver nuclei as compared with that of normal controls. Starvation also decreased the phosphorylation level of major histones in relation to normal controls. The experiment with insulin injection into fed streptozotocin-diabetic rats show ed the tendency to increase phosphorylation of 0.14M NaCl soluble proteins (130,000 dalton protein) and phenol soluble non-histone proteins (155,000 dalton protein), The phosphorylation level of histones appeared to be invariant under the experimental conditions employed here. These results suggest the possibility that the phosphorylation and dephosphorylation of 0.14M NaCl soluble proteins and H₁ histone precede those of other chromatin associated nuclear proteins, It is of interest to find that insulin signal was correlated to phosphorylation of nuclear proteins while glucagon signal dephosphorylated nuclear proteins.
단식 , 재급식(再給食)과 인슈린 주사에 따른 쥐의 간세포핵단백질(肝細胞核蛋白質)에 대한 전기영동상의 분포양상 비교
이효사,데이비드엠깁슨 한국농화학회 1979 Applied Biological Chemistry (Appl Biol Chem) Vol.22 No.3
SDS gel electrophoresis has been employed to examine the changes in distribution of three major classes of nuclear proteins extracted from isolated liver nuclei in response to refeeding of starved rats with a fat-free high carbohydrate diet and following insulin injection into streptozotocin-diabetic rats. The relative quantity of electrophoretically separated proteins in the fraction showed marked changes with 0.14M NaCl extracts, but not with histones and phenol soluble non-histone proteins. During 48h starvation at least five proteins ranging in molecular weight from 50,000 to 180,000 daltons decreased relative to normal controls while a protein with 36,000 daltons was increased. Refeeding the starved rats with a high carbohydrate diet reversed these changes over 24 h. Insulin injection into streptozotocin-diabetic rats increased levels of the set of five 0.14 M NaCl soluble proteins identified from refeeding experiment of starved rats. The 36,000 daltons protein was also diminished. These results indicate that changes in distribution of certain nuclear proteins in 0.14 M NaCl extracts are associated with the control of nuclear activity related to known insulin-signalled modulation and induction of cytosolic lipogenic enzymes.
발아초기의 콩 부위별 Lactate Dehydrogenase 활성변화 및 효소성질 비교
이효사,전태홍 한국농화학회 1983 Applied Biological Chemistry (Appl Biol Chem) Vol.26 No.1
The change of lactate dehydrogenase(LDH) activity and the possibility of the existence of LDH. isozyme were examined with different parts of soybean sprout. The enzyme activity was little changed in cotyledons throughout the early stagy of germination. However, hypocotyls and roots showed the continuous decline of the enzyme activity since the radicle emerged from seeds. It was found that LDH from hypocotyls. and roots was unstable as compared with LDH from cotyledons, even at low temperature. The enzyme from hypocotyls and roots was not purified with a good yield when the purification procedure developed for LDH from cotyledons. was employed. LDH from hypocotyls and roots has the Rm value of 0.29, and 0.25 from cotyledons. The apparent Km value for LDH from cotyledons was 0.45mM with sodium pyruvate, while crude homogenate of hypocotyls or roots showed biphasic phenomenon with two Km values 0.014 and 0.45mM. The results indicate the possibility that crude homogenate of hypocotyls or roots may contain a different LDH isozyme from the LDH of soybean reported previously.