한국산 야생쥐류에 기생하는 이(蝨)류의 숙주 특이성

백문기,배양섭,홍한기 한국곤충학회 1999 Entomological Research Vol.29 No.4

한국산 야생쥐류에 기생하는 이류의 숙주 특이성에 관하여 1989년 3월부터 1994년 8월까지 8도 7시 26군 38지역에서 실시한 결과, 한국산 야생쥐류에 기생하는 이류는 등줄쥐이 (굵은몸쥐이과), Hoplopleura acanthopus (굵은몸쥐이과), 생쥐이 (가는몸쥐이과), 집쥐이 (가는몸쥐이과), Mallophaga sp.의 2목 3과 5종으로 규명되었으며, 이 중 H. acanthopus는 대륙밭쥐, 집쥐이는 시궁쥐에 숙주 특이성을 나타냈고, 등줄쥐이와 생쥐이는 등줄쥐에 숙주 특이성을 나타냈다. Host Specificity of ectoparasitic lices of wild rodents in Korea was studied from March 1989 to August 1994. Five species belonging to three genera were collected from wild rodents during the survey and identified to be Hoplopleuridae: Hoplopleura affinis (Burmeister), H. acanthopus Ferris; Polyplacidae: Polyplax serrate (Burmeister), P. spinulosa (Burmeister); Mallophaga sp. The Specific rodent host species for the ectoparasitic lice were Eothenomys regulus for H. acanthopus, Rattus norvegicus for P. spinulosa, and Apodemus agrarius for H. affinis and P. serrata.

胞狀奇胎 組織의 Deoxyribonuclease에 關한 硏究

白汶基 全南大醫大 1969 전남의대학술지 Vol.6 No.3

哺乳動物 細胞의 膜 結合 Nucleases 에 關한 硏究 : 家兎 綱狀血球 膜 結合 Deoxyribonuclease의 精製와 그 性狀 Purification and Characterization of the Membrane-bound Deoxyribonuclease from Rabbit Reticulocytes

白汶基 충남대학교 의과대학 지역사회의학연구소 1974 충남의대잡지 Vol.1 No.1

The membrane-bound deoxyribonuclease(DNase) has partially been purified from rabbit reticulocytes, and its properties have been investigated. Evidence is presented indicating that the DNase and ribonuclease(RNase) associated with rabbit reticulocyte membrane are distinct enzyme entities. The membrane-bound DNase of rabbit reticulocytes is differentiated from reticulocyte membrane-bound RNase by Sephadex-G-200 chrcmatography. The enzyme shows optimal pH around 5 and is more heat-labile than the RNase, being inactivated over 60°. Mg^2+ inhibits the enzyme at 10 mM and 5 mM, respectively, suggesting that the enzyme activity is not dependent on divalent cations. The enzyme is activated by urea above 1M, but not influenced by p-hydroxymer-curibenzoate. The enzyme acts on both native and heat-denatured DNA with preference for the former. From the studies on the chain length of the reaction product and relationship between enzyme activity and reaction time, it is suggested that the enzyme is of an endonuclease, and belongs to DNase-II of Lindahl's classification. Some inhibitors of protein nature are suggested to be present in normal erythrocytes and reticulocytes.

胎盤組織의 Nucleases에 關한 硏究(Ⅱ) : 사람 胎盤組織의 Alkaline Deoxyribonucleases의 性狀 Properties of Alkaline Deoxyribonucleases from the Early Human Placenta

白汶基,黃炳斗,李正馥,琴基昌 충남대학교 의과대학 지역사회의학연구소 1978 충남의대잡지 Vol.5 No.1

Properties of alkaline deoxyribonucleases from cytosol and membane fractions of the early human placenta have been investigated. Evidence is indicating that the cytosol deoxyribonuclease (DNase) having an optimal pH around 9 and the plasma membrane bound DNases having an optimal pH around 8 (pH- 8-PM-DNase) and 9. 5 (pH-9.5-PM-DNase), respectively, are distinct enzyme entities. The cytosol DNase, partially purified, is activated by 1mM CO^2+ and the pH-8-PMDNase and the pH-9. 5-PM-DNase are required Mg^2+ and Co2^2+, respectively, for its maximal activity. The cytosol DNase is relatively heat-labile, whereas the plasma membrane bound DNases are heat-labile with some differnce. The above DNases act both on the native DNA and the heat-denatured DNA with preference for the latter. Kinetic analysis shows that the maximal velocity is independent of Co^2+, while Km decreases from 4. 16 × 10 exp(-4) M DNA-p in the absence of Cot^2+ to 9. 4×10 exp(-5) M DNA-p in the presence of Co^2+. From the above result and the fact that the DNA is not only associated with membrane structure, but also membrane-DNA interaction may be relevant to several pathologic process, including aging and carcinogenesis, we discussed that the PH-9-PM-DNase is related to the differenciation of the early placenta.

한국 고유종 Pisidium (Neopisidium)coreanum (산골조개)의 metallothionein 유전자를 기초로 한 분자계통 분류학적 연구

백문기,이준서,강세원,이재봉,강현정,조용훈,노미영,한연수,최상행,채성화,박홍석,이준상,이용석 한국패류학회 2009 The Korean Journal of Malacology Vol.25 No.2

Pisidium (Neopisidium) coreanum is a freshwater snail and lives in spring water near mountain areas. Interestingly, this snail has traditionally regarded as medicinal food, and thus has been used as folk remedies for healing broken bones. Recently, alpha classification on Pisidium (Neopisidium) coreanum through re-description has been conducted. However, not much attention has so far been made in beta classification. In this study, we performed the beta classification based on metallothionein (MT) genes found from various organisms. To this end, the complete cDNA sequences were obtained from the Expressed Sequence Tag (EST) sequencing project of Pisidium (Neopisidium) coreanum. The coding region (315 bp) gives an amino acid sequence of 105 residues. The combined results from BLAST analyses, multiple sequence alignment and molecular phylogenetic study of Pc-MT gene indicate that Pisidium (Neopisidium) coreanum has similarity to freshwater bivalve such as Dreissena polymorpha (zebra mussel), Unio tumidus (swollen river mussel) and Crassostrea ariakensis (suminoe oyster). Pisidium (Neopisidium) coreanum is a freshwater snail and lives in spring water near mountain areas. Interestingly, this snail has traditionally regarded as medicinal food, and thus has been used as folk remedies for healing broken bones. Recently, alpha classification on Pisidium (Neopisidium) coreanum through re-description has been conducted. However, not much attention has so far been made in beta classification. In this study, we performed the beta classification based on metallothionein (MT) genes found from various organisms. To this end, the complete cDNA sequences were obtained from the Expressed Sequence Tag (EST) sequencing project of Pisidium (Neopisidium) coreanum. The coding region (315 bp) gives an amino acid sequence of 105 residues. The combined results from BLAST analyses, multiple sequence alignment and molecular phylogenetic study of Pc-MT gene indicate that Pisidium (Neopisidium) coreanum has similarity to freshwater bivalve such as Dreissena polymorpha (zebra mussel), Unio tumidus (swollen river mussel) and Crassostrea ariakensis (suminoe oyster).

Two New Records of Phycitine Moths (Lepidoptera, Pyralidae) in Korea

백문기,차진열,배양섭 한국곤충학회 2002 Entomological Research Vol.32 No.2

Two species, Assara inouei Yamanaka and Assara pallidella Yamanaka, are newly added to the pyralid fauna of Korea, with redescriptions and illustrations of adult and genitalia.

태반조직의 Nucleases 에 관한 연구 ( 1 ) 사람 태반조직의 Deoxyribonucleases

백문기,황병두,금기창 ( Moon Kee Paik,Byung Doo Hwang,Ki Chang Kum ) 생화학분자생물학회 1976 BMB Reports Vol.9 No.1

The properties of acid deoxyribonuclease purified from human placenta have been investigated, and serial estimation of acid and alkaline deoxyribonuclease in human placenta has been performed. The acid deoxyribonuclease is partially purified forty-fold with specific activity of 240 units/㎎ protein. The acid deoxyribonuclease having an optimal pH around 5 is heat-labile with complete loss of activity at 70 for 10 minutes. The acid deoxyribonuclease is inhibited by Mg^(2+), Mn^(2+), Car and Co^(2+) above 1 mM concentration, suggesting that the enzyme is not dependent on divalent cations. The acid deoxyribonuclease acts on both native and heat-denatured DNA with preference for the former. A gradual decrease in the acid deoxyribonuclease activity occurs with advancing gestation after 20 weeks, the activity at term being about one-fourth of that before 20 weeks. The alkaline deoxyribonuclease activity is maintained untill approximately the 16th week of gestation at which the functioning villi has been established, and thereafter decreases rapidly with no apparent activity about 28 weeks. From the activity changes with gestational age, it is discussed that the acid deoxyribonuclease is related to DNA synthesis of the placenta whereas the alkaline deoxyribonuclease plays an important role in the formation of the functioning villi, suggesting that alkaline deoxyribonuclease is a useful enzyme to evaluate the function of the early placenta.

Bovine Fetal Liver Protein Methylase I의 정제와 특성

한균인,송우건,홍정희,한유정,백문기 圓光大學校 大學院 1996 論文集 Vol.16 No.-

S-/Adenosyl-L-Methionine; Protein Arginine N-Methyltransferase [Protein Methylas I, EC : 2.1.1.23]which methylates guanidino guanidino group of arginine residue was purified 1,600 fold with about 4% yield from bovine fetal liver. The purified enzyme preparation showed 3 protein bands on non-denaturing PAGE and 4 bands on SDS-PAGE having molecular weight of 97, 60, 44 and 38 kDa, respectively, indicating that one of the bnads is composed of two different size subunits. The enzyme had a pH optimum around 7.8 and was thermolabile, being inactivated completely at 50℃ for 5 min. The purified nuclei and histone H3 were good substrates. Among divalent cations tested Cu²? was the most detrimental towards the enzyme; at 50 μM for 5min, 60% of the activityh was inhibited with K? value of 4 ×10?M. The K? values for AdoMet was 4 ×10?M. Sinefungin was effective inhibitor of the enzyme with K? value of 8 ×10?M. The N-terminal amino acid sequence of 16 kDa nuclear methyl acceptor protein which had been strongly [methyl-?H]-labeled and purified from the nuclei was (¹Ala-Gly-Thr-X-?Gin-Thr-Ala-Arg-Lys-?Ser-Thr-Gly-Gly-Lys-?Ala), having 92.3% homology with histone H3. After methylating the nuclei with enzymc from each of purification step using Ado[methyl-³H]Met, nuclear methyl acceptor protein was analyzed by combined use SDS-PAGE and fluorography. Only 16 kDa nuclear protein was radiolabeled irrespective of the enzyme preparation. This suggested that a single enzyme is involved for the methylation. From the above result, the purified PM-1 appears to be 16 kDa nuclear protein specific PM-1.

S-Adenosyl-L-Methionine:Protein-Arginine N-Methyltransferase : Purification & Characterization

백문기,황병두,홍정의,임규,금기창 충남대학교 의과대학 지역사회의학연구소 1982 충남의대잡지 Vol.9 No.1

S-adenosyl-L-methionine : protein-arginine N-methyltransferase has been purified from human term placenta approximately 5,700 fold with a 11% yield. The final preparation is completely free of any other protein specific methyltran sferases. Histones appear to be a good substrate in accepting methyl group from S-adenosyl-L-methionine, whereas the relative substrate efficiency of myelin basic protein is less than 5% of that of histone IIA, indicating that the methylation of myelin basic protein is carried out by different enzyme entity. The enzyme preparation shows two optimum pHs around 7. 6 and 8. 1, and is stable in the presence of 10% glycerol when stored at -10℃, only 12% activity being lost over 8 weeks. The enzyme is, however, easily inactivated by treating the enzyme preparation at 50℃ for 7 min. The enzyme does not require any divalent cations. The divalent cations Cu^2+, Zn^2+, Co^2+, and Mn^2+ are found to be inhibitory, Cu^2+ being most potent since not only 90% of the enzyme activity is inactivated at 0.5 mM but also the activity could not be reversed by the addition of 1 mM EDTA. The enzyme activity is mainly located in the cytosol and nuclear fractions. Km value for S-adenosyl-L-methionine and Ki value for S-adenosyl-L-homocysteine are 5 × 10 exp (-6) M and 1.59 × 10 exp (-6) M respectively, and molecular weight of the enzyme deduced from Sephacryl-S-300 chromatography appears to be greater than 1.5 × 10 exp (6). The occurence of the specific enzymes responsible for the methylation of histones, nonhistone chromosomal protein and HnRNP respectively, and the possible multienzyme complex to be formed by these specific enzymes are discussed.

사람 胎盤組織의 Alkaline Deoxyribonuclease

白汶基,黃炳斗 충남대학교 의과대학 지역사회의학연구소 1976 충남의대잡지 Vol.3 No.2

Serial estimation of acid and alkaline deoxyribonucleases of human placenta has been performed, and some properties of alkaline deoxyribonuclease having an optimal pH around 9 has been investigated. A gradual decrease in the acid deoxyribonuclease activity occurs with advancing gestation after 20 weeks, the activity at term being about one fourth of that of before 20 weeks. The alkaline deoxyribonuclease activity in maintained until approximately the 16th week of gestation at which the functioning villi has been established and thereafter decreases rapidly with no apparent activity about 28 weeks. The alkaline deoxyribonuclease is heat-stable with 30% activity even at 90℃ for minutes. The alkaline deoxyribonuclease is inhibited by Ca^2+, Mn^2+ and ethylenediaminetetraacetate and is activated by Co^2+, Mg^2+, ATP and cyanocobalamin, the optimal concentration of Co^2+ necessary for maximal activity being 3 mM. The alkaline deoxyribonuclease acts both on the native DNA and heat-denatured DNA with preference for the latter. Kinetic analysis shows that the maximal velocity is independent of Co^2+ while Km decrease from 4.16 × 10^-4 M DNA-P in the absence of Co^2+ to 9.4 × 10^-5 DNA-P in the presence of Co^2+. From the activity changes with gestational age, it is suggested that the alkaline deoxyribonuclease plays an important role in the differentiation of the function villi.