• 제목/요약/키워드: dismutase

검색결과 2,441건 처리시간 0.029초

사료 내 분말 청국장이 돌돔, parrootfish, Oplegnathus fasciatus의 간 내 superoxide dismutase 활성에 미치는 영향 (Effects of Dietary Cheongkukjang on Liver Superoxide Dismutase Activity of Parrotfish Oplegnathus fasciatus)

  • ;이경준
    • 한국양식학회지
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    • 제20권2호
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    • pp.132-139
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    • 2007
  • A four-week feeding trial was conducted to investigate the effects of dietary soybean meal (SBM) and powdered Cheongkukjang (CKJ) on non-specific immune responses of parrotfish Oplegnathus fasciatus. Three isonitrogenous (42% crude protein) and isocaloric (17.1 MJ/kg) diets were formulated to replace fish meal by 0, 25% SBM or 25% CKJ (designated as FM, 25SBM and 25CKJ, respectively). Ninety fish (initial body weight 122 g) were randomly allotted into nine 150 L tanks. One of the three experimental diets was fed to triplicate groups of fish for 4 weeks. After the feeding trial, no differences were observed in growth performances and feed utilization among fish groups. Liver superoxide dismutase activity of the fish fed CKJ containing diet was significantly higher than that of the control groups. DPPH radical scavenging and $Fe^{2+}-chelating$ activities of the experimental diets containing SBM or powdered CKJ were significantly higher than that of the control diet. The results of the present study suggest that dietary inclusion of powdered 25CKJ significantly increased liver superoxide dismutase activity and did not affect the growth performances, feed utilization, morphological parameters, as well as hematological values of parrotfish.

일산화탄소 폭로후 고압산소 투여가 흰쥐 신장에서의 malondialdehyde 함량과 catalase 및 superoxide dismutase 활성에 미치는 영향 (Effects of Hyperbaric Oxygen Treatment on the Malondialdehyde Level and Activities of Catalase and Superoxide Dismutase in the Kidney of the Rats Exposed to Carbon Monoxide)

  • 신인철;강주섭;고현철;하지희
    • Biomolecules & Therapeutics
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    • 제7권2호
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    • pp.121-126
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    • 1999
  • In an attempt to define the effects of hyperbaric oxygen treatment on the lipid peroxidation and oxygen free radical reactions in rats exposed to carbon monoxide, we studied malondialdehyde (MDA) level and activities of catalase and superoxide dismutase in the kidney of the rats exposed to carbon monoxide. Male Sprague-Dawley albino rats weighing 240 to 260 gm were used. Experimental groups consist of Control group (=breathing with air), HBO group (=exposed to hyperbaric oxygen 〔HBO, 3ATA, 100%〕 after air breath), CO group (=exposed to CO〔3,970 ppm〕after air breath), CO-Air group (=exposed to CO after air breath followed by air breath) and CO-HBO group (=exposed to CO after air breath followed HBO treatment). The CO group showed significantly higher MDA level, catalase activity and SOD activity as compared to that of control group. The CO-HBO group showed significantly lower MDA level as compared to that of CO group, and did not show significantly lower catalase activity and SOD activity as compared to that of CO group. These results suggest that the excessive oxygen free radicals is an important determinant in pathogenesis of CO-induced nephrotoxicity and HBO inhibits the lipid peroxidation caused by excessive oxygen free radicals in the kidney of the rats exposed to carbon monoxide.

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오이 추출물에 존재하는 Superoxide Dismutase의 열안정성 (Thermostability of Superoxide Dismutase from Cucumber(Cucumis sativa))

  • 박인식;김은애;김기남;길지은;이민경;김석환;서정식
    • 한국식품영양과학회지
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    • 제27권6호
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    • pp.1105-1109
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    • 1998
  • The superoxide dismutase(SOD) in peeled pericarp of cucumber was most stable at pH 8.0 and relatively stabe between pH 5.0 and 9.0. The enzyme was stable up to 6$0^{\circ}C$ and retained 12% by heat treatment at 10$0^{\circ}C$ for 5 min. At pH 2.0, the peeled pericarp enzyme activity was decreased to 10% by incubation for 3 hrs. However, the enzyme activity was increased above 25% after incubating the enzyme at pH 7.0 for 6 hrs. Retention of SOD activity in cucumber by various heating methods was also measured. The residual SOD activities of peeled pericarp and whole cucumber was estimated to be 25% and 27% after blanching(2 min), respectively. The skin enzyme retained 53% of its activity after steaming (3 min). When the peeled pericarp enzyme was incubated at 4$^{\circ}C$ for 20 days, the enzyme activity remained about 81%. However, when the enzyme incubated at 3$0^{\circ}C$ for 20 days, the peeled pericarp enzyme activity decreased to 17% of its original activity. The enzyme activity of peeled pericarp cucumber was not changed after exhaustive dialysis for 3 days, which indicated that the SOD activity in cucumber seems to have molecular weight above 12,000.

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Cloning, DNA Sequence Determination, and Analysis of Growth-Associated Expression of the sodF Gene Coding for Fe- and Zn-Containing Superoxide Dismutase of Streptomyces griseus

  • Kim, Ju-Sim;Lee, Jeong-Kug
    • Journal of Microbiology and Biotechnology
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    • 제10권5호
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    • pp.700-706
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    • 2000
  • Iron- and zinc-containing superoxide dismutase (FeZnSOD) and nickel-containing superoxide dismutase (NiSOD) are cytoplamic enzymes in Streptomyces griseus. The sodF gene coding for FeZnSOD was cloned from genomic Southern hybridization analysis with a 0.5-kb DNA probe, which was PCR-amplified with facing primers corresponding to the N-terminal amino acid of the purified FeZnSOD of S. griseus and a C-terminal region which is conserved among bacterial FeSODs and MnSODs. The sodF open reading frame (ORF) was comprised of 213 amino acid (22,430 Da), and the deduced sequence of the protein was highly homologous (86% identity) to that of FeZnSOD of Streptomyces coelicolor. The FeZnSOD expression of exponentially growing S. griseus cell was approximately doubled as the cell growth reached the early stationary phase. The growth-associated expression of FeZnSOD was mainly controlled at the transcriptional level, and the regulation was exerted through the 110 bp regulatory DNA upstream from the ATG initiation codon of the sodF gene.

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Deletion of Superoxide Dismutase Gene of Bombyx mori Nuclear Polyhedrosis Virus Affects Viral DNA Replication

  • Wang, Wenbing;Song, Zhixiu;Ji, Ping;Wu, Jun;Zhang, Zhifang;He, Jialu;Wu, Xiangfu
    • International Journal of Industrial Entomology and Biomaterials
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    • 제9권2호
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    • pp.225-228
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    • 2004
  • Superoxide dismutase (SOD) is an important enzyme which catalyzes superoxide radicals to hydrogen peroxide. A Cu, Zn sod-like gene was found in Bombyx mori nuclear polyhedrosis virus encoding 151 amino acids. To demonstrate its function, a recombinant virus named dsBmNPV with deleted sod gene was constructed. It was discovered that the sod gene was not essential for viral replication. Studies on growth of budded virus in BmN cells and superoxide dismutase and catalase activities in vivo after dsBmNPV infection showed that the titer of dsBmNPV decreased obviously comparing to wild type BmNPV, the sod gene was effective on genomic DNA replication of baculovirus, the peak of SOD activity of silkworm infected with wt-BmNPV appeared between 36 and 48 hrs post infection, and with dsBmNPV, it did not appear. And the changes of CAT activity after infection were similar to SOD activity.

Changes of superoxide dismutase and glutathione peroxidase in light damaged rat retina

  • Kaidzu, Sachiko;Tanito, Masaki;Takanashi, Taiji;Ohira, Akihiro
    • Journal of Photoscience
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    • 제9권2호
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    • pp.430-432
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    • 2002
  • The changes in expression of copper-zinc superoxide dismutase (CuZn-SOD), manganese superoxide dismutase (Mn-SOD) and glutathione peroxidase (GPX) in light-damaged rat retinas were examined. Sprague-Dawley rats (male, 6-weeks-old) were maintained on a cyclic photoperiod (12 hours light and 12 hours darkness) for 2 weeks. The illumination intensity during the light period was 80 lux. To induce light damage to the retina, a high-intensity illumination (3000-lux) was applied to the animals for 24 hours. After light exposure, the animals were returned to cyclic lighting. Eyes were enucleated 12 and 24 hours after light exposure started or 1,3, and 7 days after light exposure ended. Eyes were fixed and embedded in paraffin wax. Tissues were cut into 4${\mu}{\textrm}{m}$-thick sections. Sections were immunostained using antibody against CuZn-SOD, Mn-SOD, GPX and 8-hydroxy-deoxyguanocine (8-OHdG) as oxidative stress marker. 8-OHdG was observed in the outer nuclear layer (ONL) and retinal pigment epithelium (RPE) during light exposure. In light-damaged retinas CuZn-SOD labeling was up regulated in the ONL and RPE. Mn-SOD labeling was up regulated in rod inner segments (RIS) during light exposure and that in the RPE was up regulated after exposure. GPX labeling was observed in rod outer segments (ROS) during light exposure. GPX labeling was also observed in the RPE during and after light exposure. All three enzymes were observed in the outer retina, which suffered light damage, but occurred in defferent layers except within the RPE, in which case all three were expressed. These enzymes may play complementary roles as protective factors in light-damaged retinas.

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백두산 자생참돌꽃의 생육과 이용 II. 유식물의 부위별 superoxide dismutase 활성 (Growth and Utility of Rhodiola sachalinensis in Baekdu Mountain II. Activities of Superoxide Dismutase in Portions of the Seedlings)

  • 소상섭
    • 환경생물
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    • 제26권4호
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    • pp.349-354
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    • 2008
  • 참돌꽃 유식물에서 줄기와 뿌리의 부위별로 나타나는 superoxide dismutase(SOD)의 활성과 환경 스트레스 또는 항산화분자 처리에 따른 SOD활성도를 조사하여 다음과 같은 결론을 얻었다. SOD의 활성은 줄기보다는 뿌리에서 높았고 각 기부보다는 선단부에 이를수록 높았으며 이러한 현상은 유식물 생육의 초기보다 후기에 더 상승된 결과를 나타내고 있다. 또한 환경 스트레스에 대한 SOD의 활성도는 유식을 초기생육 상태에서는 NaCl또는 cadmium(Cd) 등 유해물질 처리 후 10 및 30% 정도 저해를 받고 있으나 생육 후기에 이를수록 처리된 유해인자에 의한 산화적 스트레스에 대하여 유식물은 자체의 SOD 활성 수준이 상향되는 방어능력을 보였으며 이러한 현상은 뿌리에서 더욱 현저하였다. SOD 활성도를 높이기 위해 항산화물질로 ascorbic acid를 처리한 유식물은 생육 후 최고 46%까지 높아짐을 보였으나 동시기의 스트레스 물질로 첨가한 cadmium 처리구에서 나타난 SOD 활성도에 비하여 유의할만한 상승효과의 차이를 보이지는 않았다. 이러한 결과는 참돌꽃 유식물 특히 뿌리부위는 항산화 기질의 처리 없이도 유해한 환경 인자에 노출되면 자체의 방어 수단으로 SOD 생성이 활발히 진행되고 있음을 시사하였다.

Paraquat 저항성 망초의 protective 효소 (Protective Enzymes of Paraquat-Resistant Conyza bonariensis)

  • 김희주;황을철
    • Applied Biological Chemistry
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    • 제43권1호
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    • pp.46-51
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    • 2000
  • 망초(Conyza bonariensis)에서 제초제 paraquat 저항성을 구명하기 위해 paraquat가 생성하는 superoxide 라디칼과 과산화수소 등의 유해 산소 물질을 제거하는 데에 관련된 효소의 활성을 저항성 종과 감수성 종의 망초에서 측정하였다. 경작지 부근에 자라는 망초는 비경작지에 자라는 망초에 비해 paraquat 저항성이 강하였다. 국내에서 paraquat를 자주 살포하는 지역에서 저항성 종의 망초가 출현하고 있음을 처음으로 보고한다. 저항성 종의 superoxide dismutase의 활성, ascorbate peroxidase의 활성, 그리고 glutathione reductase의 활성은 감수성의 그것에 비해 각각 약 20%, 44%, 그리고 64% 높게 나타났다. 이러한 결과로부터 paraquat에 대한 망초의 저항성은 superoxide dismutase, ascorbate peroxidase, 그리고 glutathione reductase 등으로 구성된 효소의 유해 산소 물질을 제거하는 효율성에 부분적으로 달려 있을 수 있다고 사료된다.

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염증성 치은에서 superoxide dismutase isoform의 발현에 대한 연구 (Expression of Superoxide Dismutase Isoforms in Inflamed Gingiva)

  • 나혜진;김옥수;박병주
    • Journal of Periodontal and Implant Science
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    • 제36권1호
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    • pp.97-112
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    • 2006
  • 유리 라디칼과 활성 산소종, 산화방지제 간의 불균형이 염증성 구강내 질환의 발생과 진행에 있어 중요한 역할을 한다는 주장이 제기되었고 최근에는 만성 염증성 치주질환에서도 산화에 의한 소실이 관찰되었다. 다양한 내적인 항산화 방어 기전 중 superoxide dismutase 가 $O_2$$H_2O_2$로 효과적으로 전환시킴으로써 활성산소종에 대한 일차적인 방어를 맡고 있다. 현재까지 인간에서 발견된 superoxide dismutase 는 cytoplasmic copper-zinc SOD와 mitochondrial manganase SOD, extracellular SOD의 3가지 아형이다. 이번 연구는 만성 치주질환을 가전 환자의 치주조직에서 효소 항산화제인 SOD의 발현정도를 알아봄으로써 질환조직 내의 산화자극 정도를 평가해 보고자하였다. 전남대학교 치주과에 내원한 33명의 만성 치주질환자와 20명 의 임상적으로 건강한 대상으로부터 조직을 얻어 Cu/Zn-SOD와 Mn-SOD, EC-SOD를 이용한 면역조직화학 염색을 시행하였다. 임상적 소견과 조직학적 소견이 일치하지 않아 조직학적 소견을 기준으로 건강한 조직, 경도, 중등도, 중도 치주질환 조직으로 그룹을 나누고 완전한 상피와 결합조직을 가진 27개의 표본에 대한 분석을 시행하였다. 치주질환 조직에서 건강한 조직에 비해 Cu/Zn-SOD가 상피의 기저층과 상피에 근접한 결합조직에서 발현되고 Mn-SOD는 염증이 증가함에 따라 크게 상피의 과립증과 각화층, 그리고 상피에 근접한 결합조직에서 발현됨으로써 활성산소종이 치주조직 파괴에 관여한다는 것을 알 수 있었다. 세 아형 모두 혈관주위에서 발현되었고 특히 EC-SOD는 작은 모세혈관주위에서만 발현되었으나 염증에 의해 혈관벽이 두꺼워지고 혈관 수가 증가한 곳에서 뚜렷하게 염색되었다. 이번 연구는 염증성 치주조직내 증가된 SOD의 활성이 치주질환자의 산화자극 정도와 관련되어 있음을 시사하였다.

Salsolinol, a Tetrahydroisoquinoline Catechol Neurotoxin, Induces Human Cu,Zn-superoxidie Dismutase Modificaiton

  • Kang, Jung-Hoon
    • BMB Reports
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    • 제40권5호
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    • pp.684-689
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    • 2007
  • The endogenous neurotoxin, 1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol), has been considered a potential causative factor for the pathogenesis of Parkinson's disease (PD). In the present study, we examined the pattern of human Cu,Zn-superoxide dismutase (SOD) modification elicited by salsolinol. When Cu,Zn-SOD was incubated with salsolinol, some protein fragmentation and some higher molecular weight aggregates were occurred. Salsolinol led to inactivation of Cu,Zn-SOD in a concentration-dependent manner. Free radical scavengers and catalase inhibited the salsolinol-mediated Cu,Zn-SOD modificaiton. Exposure of Cu,Zn-SOD to salsolinol led also to the generation of protein carbonyl compounds. The deoxyribose assay showed that hydroxyl radicals were generated during the oxidation of salsolinol in the presence of Cu,Zn-SOD. Therefore, the results indicate that free radical may play a role in the modification and inactivation of Cu,Zn-SOD by salsolinol.