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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.
α - 술폰 지방산 알릴에스테르 올리고머의 합성 및 안료 분산성
이향우(Hyang Woo Lee),권순일(Soon Il Kown),남기대(Ki Dae Nam) 한국유화학회 2001 한국응용과학기술학회지 Vol.18 No.1
N/A Allylaliphatic carboxylate oligomers were prepared from polymerization giving allyl aliphatic carboxylates in the presence of potassium persulfate in methanol and the α-sulfonation of these allyl aliphatic carboxylates oligomers were carried by direct addition of dry sulfur trioxide. The dispersing performance of oligomer type anionic surfactants and SDS in the aqueous suspension of Fe_2O_3 and Tio_2 particles were evaluated by particle size distribution and ζ-potential measurement. As results, the particles of Fe_2O_3 and Tio_2 were flocculated by addition of small amount of oligomer type anionic surfactants and SDS, then the flocks redispersed by more addition oligomer type anionic surfactants and SDS. The dispersion and flocculation were observed in lower concentration range of oligomer type anionic surfactants than SDS.
토끼에서 신델라 겔 ( 송아지의 제단백혈액추출물 황산 미크로노아이신 = 20 1 혼합물 ) 의 피부자극성시험
남석우(Suk Woo Nam),이영진(Young Jin Lee),고영권(Young Kwon Ko),장만식(Man Sik Chang),최완수(Wahn Soo Choi),김규봉(Kyu Bong Kim),우태욱(Tae Wook Woo),한정환(Jeung Whan Han),홍성렬(Sung Youl Hong),이향우(Hyang Woo Lee) 한국응용약물학회 1996 Biomolecules & Therapeutics(구 응용약물학회지) Vol.4 No.4
This study was conducted to investigate the skin irritation toxicity of Syndella gel, a combination topical drug containing a deproteinised dialysate of calfs blood and micronomicin sulfate in the ratio of 20 to 1, in New Zealand White rabbits. In the primary skin irritation test with male New Zealand White rabbits, there was no treatment-related effect on clinical sign, and body weight was not significantly changed. The Primary Irritation Index (PII) was 0.33, indicating that Syndella gel was a mildly irritating formulation.
당류를 친수기로 한 비이온성 계면활성제계의 상거동 ( 제2보 ) - 슈크로오스 팔미테이트 / 알칸올 / 물 계에서의 상거동 -
이향우,이진희,남기대 ( Hyang Woo Lee,Jin Hee Lee,Ki Dae Nam ) 한국공업화학회 1997 공업화학 Vol.8 No.2
당류를 친수기로 한 슈크로오스 모노팔미테이트에 대한 3성분계 즉, 슈크로오스모노팔미테이트/알칸올/물계에서의 상거동을 각 조성에 따라 조사하였다. 미셀영역에서 여러 액정영역에 이르기까지 각 성분의 조성을 변화시키면서 정온 및 변온하에 여러 상의 구조를 온도조절기와 카메라가 부착된 편광현미경으로 비교관찰하였다. 극성물질인 알칸올의 탄소수 증가에 따른 3성분계에서의 상거동을 관찰한 결과, 헥산올<옥탄올<데칸올 순으로 비교적 넓은 영역에서 비등방성의 여러 액정상이 존재하였으며, 이를 토대로 에멀젼이나 가용화계의 포뮬레이션에 적용할 수 있다. The phase behavior of sucrose monopalmitate/alkanol/water ternary system was investigated. According to compositions of three components ranging from micellar(or inverse micellar) solution up to various lyotropic liquid crystalline(LC) phase, each texture of the separated phases was identified by crossed polarizers equipped with a camera whose stage was connected to a thermostatic circulator. As the carbon atom number in alkanol of the polar oily substance increases, patterns of the various LC phases were also observed hexanol<octanol<decanol in order, and thus could be also applied to formulation of the emulsified or solubilized systems.
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.
랫트에 있어서 신델라 겔 ( 송아지의 제단백혈액추출물 황산 미크로노마이신 = 20 1 혼합물 ) 의 피하급성독성시험
남석우(Suk Woo Nam),서동완(Dong Wan Seo),안성훈(Sung Hoon Ahn),장만식(Man Sik Chang),최완수(Wahn Soo Choi),김규봉(Kyu Bong Kim),우태욱(Tae Wook Woo),한정환(Jeung Whan Han),홍성렬(Sung Youl Hong),이향우(Hyang Woo Lee) 한국응용약물학회 1996 Biomolecules & Therapeutics(구 응용약물학회지) Vol.4 No.4
Single subcutaneous administration to S.D rats of both sexes was performed to investigate the acute toxicity of Syndella gel, a new topical drug containing deproteinised dialysate of calfs blood and micronomicin sulfate. LD_(50) values for S.D rats were 23,047 ㎎/㎏ for male and 23,725 ㎎/㎏ for female. The death occurred within 24 hours after administration at doses over 19,200 ㎎/㎏. The main cause of death seemed to be respiratory disturbance by acute shock. Major general symptoms induced by injection subcutaneously with Syndella gel were underactivity, decreased respiratory rate, salivation, tremor and loss of consciousness. No significant body weight changes and gross findings of internal organs in treatment groups in comparison with those of control groups was observed at any dose levels in Syndella gel.
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.
김원준,김혜영,이향우,홍사석,Kim, Won-Joon,Kim, Hea-Young,Lee, Hyang-Woo,Hong, Sa-Suk 대한약리학회 1980 대한약리학잡지 Vol.16 No.2
[${\alpha}$]-Amylase catalyses the hydrolysis of starch, glycogen, and related poly- and oligosac-charide by random cleavage of ${\alpha}$-D-(l-4) glucan linkage. In man large amounts of amylase are secreted into the digestive tract by the salivary and exocrine pancreatic gland, minimal amount being produced also in other tissues. It has been known that ${\alpha}$-amylase exists in multiple molecular forms, isoenzyme which can be separated from each other because of difference in their physicochemical properties. By using various methods, several groups of investigator have separated the many isoenzyme in serum, saliva and pancreatic juice. Furthermore, changes of the normal serum isoenzyme pattern is diagnostically useful even when the total serum enzyme activity is noninformative, such as the clinical use of isoenzyme of serum lactate dehydrogenase. Procarboxypeptidase-A which is one of the pancreatic enzymes is also present as isoenzymes. Four forms of procarboxypeptidase-A haye been found in the bovine enzyme and three forms of the porcine enzyme. In human pancreatic juice four forms of procarboxypeptidase-A isoenzyme were found by isoelectric focusing method. Recently, the so-called isoamylase analysis was developed for the diagnostic use of amylase in pancreatic diseases. In alcohotic patients, the serum concentration of pancreatic isoamylase is subnormal and this lowered activity provides strong evidence for pancreatic exocrine insufficiency. The purpose of this study was to elucidate the variations of the isoenzyme of amylase and procarboxypeptidase-A in serum, saliva and pancreatic juice of the experimental animals. The results are as follow. 1) Three main forms of isoenzyme of amylase by isoelectric focusing were found in pancreatic juice of normal rabbit. However, many new bands were appeared in the pancreatic juice of cholic acid administered animal intravenously while the infusion of cholic acid or elastase into pancreatic duct produced the decrease of number of the fractions on the isoelectric focusing. In the case of serum isoenzyme from normal animal, two major and a few minor isoamylases were observed. By injecting alcohol intravenousely the fractions of serum isoamylase were significantly decreased and in contrary to the pattern in the pancreatic juice the infusion of cholic acid or elastase into pancreatic duct exhitited a significant decrease of the isoenzyme of amylase fractions. In saliva from normal animal three main isoamylase were produced of the administration of alcohol. 2) In the case of procarboxypeptidase-A isoenzyme, two major fractions which have isoelectric point at 6.2 and 6.4 and other two minor bands were observed in the pancreatic juice of normal rabbit. By the treatment of the juice with trypsin, only one band was produced on the isoelectric focusing. No procarboxypeptidase was appeared on the electrofocusing by the infusion of cholic acid or phospholipase A into the pancreatic duct of rabbit. However, a single major fraction of procarboxypeptidase-A was appeared at 3 hr after simple ligation of the pancreatic duct. No significant changes were observed in the juice of the alcohol or cholic acid administered group.
남석우(Suk Woo Nam),박승희(Seung Hee Park),윤성필(Sung Pil Yoon),서동완(Dong Wan Seo),남태균(Tae Kyun Nam),홍성렬(Sung Youl Hong),이향우(Hyang Woo Lee) 한국응용약물학회 1995 Biomolecules & Therapeutics(구 응용약물학회지) Vol.3 No.2
Effects of Biozyme^R and Business^R on alcohol metabolism in rats, and on the activities of alcohol dehydrogenase(ADH) and acetaldehyde dehydrogenase(ALDH) were studied in vitro. Alcohol concentration in rat blood was decreased after the treatment of Business(3.3 ㎖/㎏, Biozyme 1.67 ㎎/㎖) and Biozyme(3.3 ㎖/㎏, 1.67 ㎏/㎖) prior to the administration of ethanol(25%, 0.83 g/㎏). And the acetaldehyde concentration of rat blood was also decreased when compared with control values in the same condition. Effects of Biozyme on ADH and ALDH activity were also studied. While the ALDH activity was elevated in the presence of Biozyme(2 ㎍/assay), the ADH activity was not influenced by Biozyme at the concentration range from 2 ㎍/assay to 0.2 ㎎/assay. In summary, Biozyme accelerated the rate of ethanol metabolism and the acceleration might be due to the increase in ALDH activity.