• Title/Summary/Keyword: Cytochrome Oxidase I

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Toxic action of benfuracarb via oxidative bioactivation process by cytochrome $P_{450}$ (Procarbamate계 살충제 benfuracarb의 산화적 활성화 과정을 통한 독성발현)

  • Yu, Yong-Man;Kim, Eun-H.;Kim, Song-Mum;Hur, Jang-Hyun
    • The Korean Journal of Pesticide Science
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    • v.7 no.1
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    • pp.45-50
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    • 2003
  • This study was conducted to understand the role of oxidative enzyme cytochrome $P_{450}$ in the bioactivation of benfuracarb and to know metabolites of benfuracarb by cytochrome $P_{450}$. The bimolecular imhibition rate constant $(k_i)$ of benfuracarb on acetylcholinesterase (AChE) was as low as $1.1{\times}10^3\;M^{-1}\;min^{-1}$, suggesting that benfuracarb should be activated for its toxic action. The potency of benfuracarb on AChE in the oxidase system (cytochrome $P_{450}$ + NADPH) in vitro was 10-fold higher than that of control (cytochrome $P_{450}$). Such a similar result was also found in the oxidase + PBO system. In vivo the $I_{50}$ of benfuracarb was 22.7mg $kg^{-1}$, but pie-treatment of piperonyl butoxide (PBO) reduced the $I_{50}$ by >100mg $kg^{-1}$. This result suggests that cytochrome $P_{450}$ was involved in the activation of benfuracarb. Using microsomal oxidase system, metabolites of benfuracarb were elucidated. Fifty-eight percent of benfuracarb was converted to carbofuran, a major toxic metabolite, in the oxidase system, while only less than two percent of benfuracarb was converted to carbofuran in the oxidase + PBO system. These results also suggest that cytochrome $P_{450}$ was involved in the activation of benfuracarb. Overall results indicate that cytochrome $P_{450}$ could be involved in the bioactivation of benfuracarb to carbofuran.

A Study on the Distribution of Cytochrome-c-oxidase Subunit in the Cristae of Mitochondria (미토콘드리아 크리스테에 존재하는 cytochrome-c-oxidase의 단백질 소단위 분포에 관한 연구)

  • Kim, Soo-Jin;Lee, Ji-Hyon;Chung, Cha-Kwon
    • Applied Microscopy
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    • v.24 no.4
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    • pp.41-51
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    • 1994
  • The topology of the enzyme has been investigated by biochemical studies including chemical labeling and cross linking. Thirteen subunits(polypeptides) of the cytochrome-c-oxidase have localistic characteristics of existing in the matrix side or cytoplasmic side in the mitochondria. In order to observe the distribution of the enzyme subunit on the mitochondria membrane, immunogold-labeling methods were employed. Antibody was obtained from the serum of immunized rabbit with enzyme subunit antigen which was obtained from cytochrome-c-oxidase of the beef heart muscle mitochondria. Beef heart muscle tissue as a tissue antigen was stained with immunized rabbit IgG and protein A gold complex. Electron microscopy has identified the existance of cytochrome-c-oxidase subunit $Mt_I,\;Mt_{II}\;and\;Mt_{III}$ on the membrane of cristae and outer chamber of mitochondria and the subunit $C_{IV}$ on the membrane of cristae and matrix of mitochondria. Particularly, the subunit $C_{IV}$ was also observed to exist in the sarcoplasm of muscle tissue.

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Comparative Study on Cytochrome Oxidase of Rat Muscle Tissues (쥐 근조직의 Cytochrome Oxidase에 대한 비교 연구)

  • Song, Eun-Sook
    • The Korean Journal of Zoology
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    • v.29 no.1
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    • pp.70-74
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    • 1986
  • Cytochrome oxidase activities have been compared from crude sumibitochondrial preparations of rat skeletal muscle tissues. Fast red (type $II_A$) preparation has highest cytochrome oxidase activity, slow red (type I) next, and fast white (type $II_B$) the lowest. Differences of electrophoretic mobilities have been detected by heme staining. Migration of heme band is in the order of slow red>fast red>fast white from fastest to slowest. Results of immunoelectrophoresis have substantiated the above finding.

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Cytochrome Oxidase Subunit II (COII) Sequence Analysis of Root-knot Nematode, Meloidogyne sp. HSC, Infesting Yam (Dioscorea bulbifera) (둥근마(Dioscorea bulbifera)를 가해하는 뿌리혹선충(Meloidogyne sp. HSC)의 Cytochrome Oxidase Subunit II (COII) 염기서열 분석)

  • Han, Sang-Chan;Kang, Sang-Jin;Kim, Yong-Gyun
    • Korean journal of applied entomology
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    • v.46 no.1 s.145
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    • pp.169-173
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    • 2007
  • Root-knot nematode damage was found on yam, Dioscorea bulbifera in Andong Korea. From the root-knots, female nematodes were isolated and subjected to DNA sequence analysis. Sequence of cytochrome oxidase subunit II (COII) was analyzed from the genomic DNA of the isolate. COII locus size and sequence of the nematode isolate were similar to those of Meloidogyne javanica or M. incognita. However, an analysis of HinfI restriction site, a species-specific character between these two species, showed that the isolate did not match to either M. javanica or M. incognita.

Effect of Butylated Hydroxytoluene and 2-Acetylaminofluorene Administration and Microsomal Mixed Function Oxidase System in Young Rats fed different Fats (Butylated Hydroxytoluene첨가 식이 및 2-Acetylaminofluorene 투여가 식이지방을 달리한 쥐간의 Microsomal Mixed Function Oxidase계에 미치는 영향)

  • 윤은영
    • Journal of Nutrition and Health
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    • v.23 no.1
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    • pp.11-18
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    • 1990
  • Sprague-Dawley male rats were fed the diet of p/s 4.0(soybean oil : I), p/s 0.08(Beef tallow : II) at the level of 15% fat until 8 weeks after weaning. I & II groups were divided into 4 sub-groups by diets with or without 0.3% butylated hydroxytoluene(BHT). 2-AAF was injected at the age of $5_{1/2}$, 6, $5_{1/2}$, 7 weeks. MFO system enzyme(cytochrome p-450, cytochrome p-450 reductase, cytochrome b5) activities and lipid peroxide were determined from isolated liver microsome. 2-AAF injected young rats had growth retardatiion. Lipid peroxide values were not influenced greatly by dietary fat, 2-AAF and BHT. Cytochrome p-450 contents were increased in I-BHT-AAF & II-AAF groups by 2-AAF and its contents were not affected by BHT. But cytochrome p-450 and cytochrome p-450 reductase were not increased in soybean oil diet ybean oil groups. Cytochrome b5 was not influenced by dietary fat, 2-AAF and BHT. Cytochrome p-450 and lipid peroxide, cytochrome p-450 reductase and cytochrome b5, which transfer to MFO system, appeared to have positive correlations(r=0.2474, r=0.2475, p<0.05) each other. This result suggests that MFO system metabolizing 2-AAF was influenced by dietary fats and BHT. 2-AAF induced growth retardation in young rats.

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Phylogenetic Analysis of Reticulitermes speratus using the Mitochondrial Cytochrome C Oxidase Subunit I Gene

  • Cho, Moon-Jung;Shin, Keum;Kim, Young-Kyoon;Kim, Yeong-Suk;Kim, Tae-Jong
    • Journal of the Korean Wood Science and Technology
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    • v.38 no.2
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    • pp.135-139
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    • 2010
  • Reticulitermes speratus is commonly found in Asia, including Korea and Japan. We recently analyzed the 5' region of mitochondrial cytochrome c oxidase subunit I to perform a phylogenetic analysis of R. speratus KMT1, isolated in Seoul, Korea. Our results, using COXI, suggest that the taxonomy of R. speratus should be reconsidered with regard to the subgenus group. A similar phylogenetic analysis by COXI and COXII demonstrated the reliability of COXI genetic information in a molecular phylogenetic analysis of termites.

Stock Characterization of the Fleshy Prawn (Penaeus chinensis) in the Yellow Sea by Intraspecific Sequence Variation of the Cytochrome c Oxidase Subunit I Gene

  • HWANG Gyu-Lin
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.29 no.6
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    • pp.876-881
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    • 1996
  • To determine the amount of genetic variation among populations of Penaeus chinensis (Osbeck) in the Yellow Sea, 342 bp region of the mitochondrial cytochrome c oxidase subunit I gene was amplified and sequenced. Six haplotypes, which differ by from one to four nucleotide sustitutions, were detected from 34 individuals of 4 populations examined. Mean sequence divergence between pairs of haplotypes was $0.68\%$. Most individuals from 4 populations were shared by the most common genotype. This genotype was distributed evenly in the Korean and Chinese populations. This result is in accordance with findings observed using RFLPs analysis of mtDNA (Hwang et al., 1997). Therefore, it is suggested that P. chinensis should be treated as one unit stock in the Yellow Sea.

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Changes in Cytochrome c Oxidase and NO in Rat Lung Mitochondria Following Iron Overload

  • Kim, Min-Sun;Hong, Min-A;Song, Eun-Sook
    • Animal cells and systems
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    • v.13 no.2
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    • pp.105-112
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    • 2009
  • In this study, the effects of iron on cytochrome c oxidase (CcO) in rat lung mitochondria were examined. Similar to liver mitochondria, iron accumulated considerably in lung mitochondria (more than 2-fold). Likewise, the reactive oxygen species and nitric oxide (NO) content of mitochondria were increased by more than 50% and 100%, respectively. NO might be produced by nitric oxide synthase (NOS), eNOS and iNOS type, with particular contribution by NOS in mitochondria. The respiratory control ratio of iron overloaded lung mitochondria dropped to nearly 50% due to increased state 4. Likewise, cytochrome c oxidase activity was lowered significantly to approximately 50% due to excess iron. Real-time PCR revealed that the expression of isoforms 1 and 2 of subunit IV of CeO was enhanced greatly under excess iron conditions. Taken together, these results show that oxidative phosphorylation within lung mitochondria may be influenced by iron overload through changes in cytochrome c oxidase and NO.

Genetic diversity of the Asian shore crab, Hemigrapsus sanguineus, in Korea and Japan inferred from mitochondrial cytochrome c oxidase subunit I gene

  • Yoon, Moon-Geun;Hong, Sung-Eic;Nam, Yoon-Kwon;Kim, Dong-Soo
    • Animal cells and systems
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    • v.15 no.3
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    • pp.243-249
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    • 2011
  • The genetic diversity and population history of the Asian shore crab, Hemigrapsus sanguineus, were investigated with a nucleotide sequence analysis of 536 base pairs (bp) of the mitochondrial cytochrome c oxidase subunit I gene (COI) in 111 samples collected from four populations in Korea and one in Japan. In total, 28 haplotypes were defined by 27 variable nucleotide sites in the COI region examined. The observed haplotypes had a shallow haplotype genealogy and no geographical associations. Most of the populations had high haplotype diversity (0.656-0.788) and low nucleotide diversity (0.00165-0.00244), and significant negative values for Fu's $F_S$, suggesting rapid and recent population growth from an ancestral population and sudden population expansion. The pairwise fixation indices ($F_{ST}$) estimated with the exact test and the migration rates indicate that substantial gene flow occurs among these populations as a result of sea currents, except between the Yellow Sea coast of Korea (BUA) and the Pacific Ocean coast of Japan (JPA). These two populations (BUA and JPA) showed significant genetic differentiation and low migration rate.

Involvement of Cytochrome c Oxidase Subunit I Gene during Neuronal Differentiation of PC12 Cells

  • Kang, Hyo-Jung;Chung, Jun-Mo;Lee, See-Woo
    • BMB Reports
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    • v.30 no.4
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    • pp.285-291
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    • 1997
  • It is becoming increasingly evident that significant changes in gene expression occur during the course of neuronal differentiation. Thus, it should be possible to gain information about the biochemical events by identifying differentially expressed genes in neuronal differentiation The PC12 cell line is a useful model system to investigate the molecular mechanism underlying neuronal differentiation and has been used extensively for the study of the molecular events that underlie the biological actions of nerve growth factor (NGF). In this study, we report an application of the recently described mRNA differential display method to analyze differential gene expression during neuronal differentiation. Using this technique, we have identified several cDNA tags expressed differentially during neuronal differentiation. Interestingly, one of these clones was cytochrome c oxidase subunit I (COX I) gene. The differential expression of COX I gene was confirmed by Northern blot analysis as well as RT-PCR. Southern blot analysis of the genomic DNA of PC12 cells revealed that COX I is a single gene. Induction of the oxidative enzyme might reflect the energy requirement in neuronal differentiation.

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