• 제목/요약/키워드: metal-binding proteins

검색결과 48건 처리시간 0.024초

METALLOTHIONEIN GENE EXPRESSION BY CADMIUM IN CRUCIAN CARP (CARASSIUS AURATUS)

  • Nam, Seong-Sook;Heekyung Bae;Kim, Eunkyoung;Moon, Chang-Kiu;Jeon, Seong-Hwan;Na, Jin-Gyun;Park, Kwangsik
    • 한국독성학회:학술대회논문집
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    • 한국독성학회 2002년도 Current Trends in Toxicological Sciences
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    • pp.127-127
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    • 2002
  • Methallothioneins(MTs) are low-molecular-mass cysteine-rich metal-binding proteins with high affinity for heavy metal ions, found in a large variety of organisms. Although the biological functions of MTS have not been fully elucidated, they are thought to play an important role in detoxification of toxic elements such as cadmium and mercury.(omitted)

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Metallothionein gene expression in different tissues of Crucian carp (Carassius auratus) exposed to cadmium chloride

  • Park, Kwang-Sik;Bae , Hee-Kyung;Nam, Seong-Sook;Kim, En-Kyoung
    • 대한약학회:학술대회논문집
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    • 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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    • pp.295.1-295.1
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    • 2002
  • Metallothioneins (MTs) are a go up of heavy metal-binding proteins characterized by cystein-rich low molecular weight(6000 - 10.000 Da). They plays a major role in the detoxification of heavy metals and also in scavenging of superoxide radicals. They are known to be induced by heavy metals in various organs of different species and represent a potential biomarker of aquatic heavy metal contamination. (omitted)

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카테콜 치환체를 가진 세파로스포린계 항생제 LB10522의 작용기전 (Action Mechanism of LB10522, a New Catechol-Substituted Cephalosporin)

  • 김무용;오정인;백경숙;김인철;곽진환
    • 약학회지
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    • 제40권1호
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    • pp.102-111
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    • 1996
  • LB10522 is a new parenteral broad spectrum cephalosporin with a catechol moiety at C-7 position of beta-lactam ring. This compound can utilize tonB-dependent iron transp ort system in addition to porin proteins to enter bacterial periplasmic space and access to penicillin-binding proteins (PBPs) which are the lethal targets of ${\beta}$-lactam antibiotics. The chelating activity of LB10522 to metal iron was measured by spectrophotometrically scanning the absorbance from 200 to 900nm. When $FeCl_3$ was added, optical density was increased between 450 and 800nm. LB10522 was more active against gram-negative strains in iron-depleted media than in iron-replete media. This is due to the increased expression of iron transport channels in iron-depleted condition. LB10522 showed a similar activity against E. coli DC2 (permeability mutant) and E. coli DCO (wild type strain) in both iron-depleted and iron-replete media, indicating a minimal permeaility barrier for LB10522 uptake. LB10522 had high affinities to PBP 3 and PBP 1A, 1B of E. coli. By blocking these proteins, LB10522 caused inhibition of cell division and the eventual death of cells. This result was correlated well with the morphological changes in E. coli exposed to LB10522. Although the in vitro MIC of LB10522 against P. aeruginosa 1912E mutant (tonB) was 8-times higher than that of the P. aeruginosa 1912E parent strain, LB10522 showed a similar in vivo protection efficacy against both strains in the mouse systemic infection model. This result suggested that tonB mutant, which requires a high level of iron for normal growth, might have a difficulty in surviving in their host with an iron-limited environment.

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Chromophorylation of a Novel Cyanobacteriochrome GAF Domain from Spirulina and Its Response to Copper Ions

  • Jiang, Su-Dan;sheng, Yi;Wu, Xian-Jun;Zhu, Yong-Li;Li, Ping-Ping
    • Journal of Microbiology and Biotechnology
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    • 제31권2호
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    • pp.233-239
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    • 2021
  • Cyanobacteriochromes (CBCRs) are phytochrome-related photoreceptor proteins in cyanobacteria and cover a wide spectral range from ultraviolet to far-red. A single GAF domain that they contain can bind bilin(s) autocatalytically via heterologous recombination and then fluoresce, with potential applications as biomarkers and biosensors. Here, we report that a novel red/green CBCR GAF domain, SPI1085g2 from Spirulina subsalsa, covalently binds both phycocyanobilin (PCB) and phycoerythrobilin (PEB). The PCB-binding GAF domain exhibited canonical red/green photoconversion with weak fluorescence emission. However, the PEB-binding GAF domain, SPI1085g2-PEB, exhibited an intense orange fluorescence (λabs.max = 520 nm, λfluor.max = 555 nm), with a fluorescence quantum yield close to 1.0. The fluorescence of SPI1085g2-PEB was selectively and instantaneously quenched by copper ions in a concentration-dependent manner and exhibited reversibility upon treatment with the metal chelator EDTA. This study identified a novel PEB-binding cyanobacteriochrome-based fluorescent protein with the highest quantum yield reported to date and suggests its potential as a biosensor for the rapid detection of copper ions.

Evaluation of Th1/Th2-Related Immune Response against Recombinant Proteins of Brucella abortus Infection in Mice

  • Im, Young Bin;Park, Woo Bin;Jung, Myunghwan;Kim, Suk;Yoo, Han Sang
    • Journal of Microbiology and Biotechnology
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    • 제26권6호
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    • pp.1132-1139
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    • 2016
  • Brucellosis is a zoonotic disease caused by Brucella, a genus of gram-negative bacteria. Cytokines have key roles in the activation of innate and acquired immunities. Despite several research attempts to reveal the immune responses, the mechanism of Brucella infection remains unclear. Therefore, immune responses were analyzed in mice immunized with nine recombinant proteins. Cytokine production profiles were analyzed in the RAW 264.7 cells and naive splenocytes after stimulation with three recombinant proteins, metal-dependent hydrolase (r0628), bacterioferritin (rBfr), and thiamine transporter substrate-binding protein (rTbpA). Immune responses were analyzed by ELISA and ELISpot assay after immunization with proteins in mice. The production levels of NO, TNF-α, and IL-6 were time-dependently increased after having been stimulated with proteins in the RAW 264.7 cells. In naive splenocytes, the production of IFN-γ and IL-2 was increased after stimulation with the proteins. It was concluded that two recombinant proteins, r0628 and rTbpA, showed strong immunogenicity that was induced with Th1-related cytokines IFN-γ, IL-2, and TNF-α more than Th2-related cytokines IL-6, IL-4, and IL-5 in vitro. Conversely, a humoral immune response was activated by increasing the number of antigen-secreting cells specifically. Furthermore, these could be candidate diagnosis antigens for better understanding of brucellosis.

물리화학적 전처리에 의한 중금속 내성세균의 균체내 중금속 축적 변화 (Heavy Metal Accumulation in Cell of Heavy Metal-Tolerant Bacteria by Some Physical and Chemical Treatments)

  • 조주식;이홍재;허종수
    • 한국환경농학회지
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    • 제16권4호
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    • pp.311-319
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    • 1997
  • 광산폐수, 산업폐수등으로 부터 Cd, Pb, Zn 및 Cu등의 중금속에 강한 내성을 지니고 있을 뿐만 아니라 균체내 중금속 축적능력이 우수한 중금속 내성 미생물 균주 Pseudomonas putida(Cd), Pseudomonas aeruginosa(Pb), Pseudomonas chlororaphis(Zn) 및 Pseudomonas stutzeri(Cu)를 각각 분리하여, 여러가지 물리화학적인 방법으로 세포를 전처리하여 세포구성성분을 인위적으로 조절한 후 세포내 중금속이온의 흡수 거동 및 조단백질 함량과 중금속 축적관계를 조사한 결과는 다음과 같다. 세포를 알카리로 전처리하였을 경우 세포내 중금속 축적은 매우 감소되었으며, 메탄올과 클로포름으로 전처리하였을 경우에는 중금속 축적에 큰 영향을 미치지 않았으나, 메탄올과 클로로포름으로 전처리한 후 다시 알카리로 재차 처리하였을 경우에는 중금속 축적이 매우 감소되었다. 전처리된 세포내 중금속 축적은 용출되지 않고 남아있는 조단백질 함량이 감소됨에 따라 더 얼마나 크게 감소되었으므로 세포 구성물질중 단백질이 중금속 축적에 중요한 역할을 하는 물질인 것으로 판단되었다.

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다양한 교정용 브라켓 표면에 부착하는 타액단백질에 관한 연구 (Adherence of Salivary Proteins to Various Orthodontic Brackets)

  • 안석준;임종안;남동석
    • 대한치과교정학회지
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    • 제32권6호
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    • pp.443-453
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    • 2002
  • 본 연구의 목적은 다양한 교정용 브라켓의 표면에 형성되는 타액성 피막의 조성을 확인하고, 전타액, 악하선타액 및 이 하선타액에서 유래하는 타액성 피막의 성분을 비교하는 것이다. 네 가지 서로 다른 종류의 교정용 브라켓을 본 연구에 사용하였다. 이들은 $022{\times}028$ Roth Prescription의 상악 소구치 브라켓으로 조성은 다음과 같다: 스테인레스 스틸, 단결정 사파이어, 다결정 알루미나 및 플라스틱 브라켓. 교정용 브라켓을 각각 전타액, 이하선타액 및 악하선타액에 2시간 배양하여 타액성 피막을 형성시켰다 브라켓 피막의 타액성분은 sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Western transfer method 및 면역검출법을 통해 확인하였다. 이 결과 low-molecular weight salivary mucin, ${\alpha}-amylase$, secretory IgA (sIgA), acidic proline-rich proteins, cystatins 등이 모든 브라켓의 타액성 피막에 존재하였으며, 치아우식증의 원인균인 Streptococcus mutans의 부착을 촉진시키는 타액단백질인 high-molecular weight mucin은 어떤 브라켓에도 부착하지 않았다. 그러나, 비록 동일한 타액단백질이 모든 브라켓에서 발견되었지만, 타액단백질 부착 양상은 타액의 종류 및 브라켓의 종류에 따라 양적 및 질적으로 다르게 나타났다. 특히 sIgA는 이하선타액에서 유래한 브라켓 피막에 더 많이 부착하였고, cystatins의 경우는 플라스틱 브라켓에서 유래한 브라켓 피막에 더 많이 존재하였다 본 연구는 다양한 타액단백질이 교정용 브라켓에 부착하며, 타액단백질이 타액의 출처 및 브라켓의 종류에 따라 교정용 브라켓의 표면에 선택적으로 부착함을 나타내었다.

Comparative and Structural Analysis of the Interaction between β-Lactoglobulin type A and B with a New Anticancer Component (2,2'-Bipyridin n-Hexyl Dithiocarbamato Pd(II) Nitrate)

  • Divsalar, A.;Saboury, A.A.;Mansoori-Torshizi, H.;Hemmatinejad, B.
    • Bulletin of the Korean Chemical Society
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    • 제27권11호
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    • pp.1801-1808
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    • 2006
  • The interaction between whey carrier protein $\beta$-lactoglobulin type A and B (BLG-A and -B) and 2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate (BPHDC-Pd(II)), a new heavy metal complex designed for anticancer property, was investigated by fluorescence spectroscopy combined with chemometry and circular dichroism (CD) techniques. A strong fluorescence quenching reaction of BPHDC-Pd(II) to BLG-A and -B was observed. Hence, BPHDC-Pd(II) complex can be bound to both BLG-A and -B, and quench the fluorescence spectra of the proteins. The quenching constant was determined using the modified Stern-Volmer equation. The binding parameters were evaluated by fluorescence quenching method. The results of binding study provided evidences presence of two and three sets of binding sites on the BLG-B and -A, respectively, for BPHDC-Pd(II) complex. Using fluorescence spectroscopy and chemometry, the ability of BLG-A and -B to form an intermediate upon interaction with BPHDC-Pd(II) complex was assessed. CD studies displayed that under influence of different concentrations of BPHDC-Pd(II) complex, the regular secondary structure of BLG-B had no significant changes, whereas for BLG-A a transition from $\alpha$-helix to $\beta$-structure was appeared. The results for both of BLG-A and -B displayed that BPHDC-Pd(II) complex can induce a conformational transition from the native form to an intermediate state with a slightly opened conformation, which is detectable with chemometry analyses.

총알고둥에서 카드뮴과 아연의 축적과 제거 (Accumulation and Elimination of Cadmium and Zinc in Littorina brevicula)

  • 한수정;이인숙
    • The Korean Journal of Ecology
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    • 제24권1호
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    • pp.35-43
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    • 2001
  • 카드뮴과 아연에 각각 그리고 동시에 노출한 총알고둥(Littorina brevicula)에서 중금속의 생체내 축적, 제거 및 세포내 분포 양상을 조사하였다. 총알고둥을 카드뮴 400 $\mu\textrm{g}$/L 또는 아연 3000 $\mu\textrm{g}$/L에 각각 90일간 노출하였을 경우, 각 중금속의 축적량은 노출기간에 따라 증가하였으며, 70일 이후에는 더 이상 축적량이 증가하지 않았다. 카드뮴과 아연을 동시에 노출하였을 경우에는 각각의 중금속에 노출하였을 경우에 비해 아연의 축적량은 증가하였으나, 카드뮴의 축적량은 감소하였다. 노출실험에 이어 수행한 42일간의 청장실험 결과, 카드뮴은 체외로 제거되지 않았으나, 아연은 제거되었다. 특히 카드뮴과 아연에 동시 노출한 총알고둥의 경우에 아연은 더 신속히 제거되었다. 총알고둥을 카드뮴과 아연에 각각 70일 동안 노출한 후, 체내로 흡수된 카드뮴의 약 60%가 soluble fraction에 분포하고 있었으며, 아연의 75%는 insoluble fraction에 분포하고 있었다. 이러한 경향은 카드뮴과 아연의 동시 노출시에도 유사하게 나타났다. 카드뮴과 아연은 soluble part내의 리간드(ligand) 와의 결합 양상에서도 차이를 나타냈는데, 카드뮴은 90% 이상이 약 6.5 kDa크기의 MBP-1(Metal-Binding Protein-1)과 결합하고 있었으나, 아연은 HMW(High molecular weight fraction, >60 kDa), MBP-1, MBP-2, LMW(Low molecular weight fraction <1 kDa)에 고루 분포하는 것으로 나타났다.

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카드뮴 유도 잉어 혈액으로부터의 Metallothionein 정제 및 이에 대한 다클론 항체 생산 (Purification of Carp Serum Metallothionein Induced in Carp with Cadmium and Production of Polyclonal Antibody)

  • 유형석;강호준;김슬기;김남수;김우연
    • 산업식품공학
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    • 제13권4호
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    • pp.314-319
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    • 2009
  • Metallothioneins (MTs) are low molecular weight, cysteine-rich, and heavy metal binding proteins, which could be induced with heavy metals such as Cd, Hg, Zn and Cu in liver, kidney, and in cultured cells. By using ion exchange chromatography on DE-52, MT was purified from the serum of carp induced with cadmium in order to produce antibody against MT. Polyclonal antibody produced against purified carp MT reacted well with MT in the serum of carp induced with cadmium, whereas control serum did not. This may indicate that the polyclonal antibody against the carp MT could be used for the preparation of biosensors to detect MT in fishes like carp.