981 resultados para CU-2
Resumo:
Cu~(2+),In~(3+),HSeO_2~+CuInSe_2.,.,,,.,.
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(n-C_(16)H_(33)NH_3)_2MX_4(C_(16)MX)n-C_(16)H_(33)NH_3X(C_(16)X)400050cm~(-1),N-HX,C_(16)XC_(16)MXCl>Br>IC_(16)MXCu~(2+)(Cu~(2+)Cd~(2+)Mn~(2+))Zn~(2+)(Zn~(2+)Co~(2+)),,MX
Resumo:
X,RBa_2Cu_3O_7-[R=LaNdSmGdDyErYb(DyYb)](Cu~(3+)/Cu~(2+)),(abcv),Cu~(3+)/Cu~(2+)()(7-)(a-b),XRD001,SEM
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Y_(1-x)Ca_xBa_2Cu_3O_(7-y),x0.15,123,,,T_cCu(2)-O,Cu(2)-O
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LaNd YbBa_2Cu_3O(7-) Yb (0.1) YbBa_2Cu_3O(7-), Cu~(3+)/Cu~(2+)
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Heat shock protein 22 (HSP22) is an important member of small heat shock protein (sHSP) subfamily which plays a key role in the process of protecting cells, facilitating the folding of nascent peptides, and responding to stress. In the present study, the cDNA of HSP22 was cloned from Argopecten irradians (designated as AiHSP22) by rapid amplification cDNA end (RACE) based on the expressed sequence tags (ESTs). The full-length cDNA of AiHSP22 was of 1,112 bp, with an open reading frame of 588 bp encoding a polypeptide of 195 amino acids. The deduced amino acid sequence of AiHSP22 showed high similarity to previously identified HSP22s. The expression patterns of AiHSP22 mRNA in different tissues and in haemocytes of scallops exposed to Cd2+, Pb2+ or Cu2+ were investigated by real-time quantitative RT-PCR. The mRNA of AiHSP22 was constitutively expressed in all examined tissues, including haemocyte, muscle, kidney, gonad, gill and heart. The expression level in heart and muscle was higher than that in other tissues. The mRNA level of AiHSP22 in haemocytes was up-regulated after a 10 days exposure of scallops to Cu2+, Pb2+ and Cd2+. However, the expression of AiHSP22 did not increase linearly along with the rise of heavy metal concentration. Different concentrations of the same metal resulted in different effects on AiHSP22 expression. The sensitive response of AiHSP22 to Cu2+, Pb2+ and Cd2+ stress indicated that it could be developed as an indicator of exposure to heavy metals for the pollution monitoring programs in aquatic environment.
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In this work, the characterization of a chitosanase-producing bacterium isolated from soil was reported and this strain was grouped under the genus Aeromonas by virtue of its morphological, physiological properties and 16S rDNA gene sequences. It is the first report that the genus Aeromonas could produce chitosanase. Aeromonas sp. HG08 could secrete the chitosanase ( named AsChi) with molecular weight of 70 kDa. The optimum pH and temperature of AsChi was 6.0 and 55 degrees C, respectively. The activity of AsChi was markedly enhanced by Mn2+ and inhibited by Fe3+, Cu2+, Ag+ and Hg2+; additionally, the activity of AsChi was increased with the degree of deacetylation ( DDA) of chitosan. Through viscosimetric assay, AsChi probably hydrolyzed chitosan in an endo-type fashion.
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Marine bacterium Vibrio sp. F-6, utilizing agarose as a carbon source to produce agarases, was isolated from seawater samples taken from Qingdao, China. Two agarases (AG-a and AG-b) were purified to a homogeneity from the cultural supernatant of Vibrio sp. F-6 through ammonium sulfate precipitation, Q-Sepharose FF chromatography, and Sephacryl S-100 gel filtration. Molecular weights of agarases were estimated to be 54.0 kDa (AG-a) and 34.5 kDa (AG-b) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH values for AG-a and AG-b were about 7.0 and 9.0, respectively. AG-a was stable in the pH range of 4.0-9.0 and AG-b was stable in the pH range of 4.0-10.0. The optimum temperatures of AG-a and AG-b were 40 and 55 degrees C, respectively. AG-a was stable at temperature below 50 degrees C. AG-b was stable at temperature below 60 degrees C. Zn2+, Mg2+ or Ca2+ increased AG-a activity, while Mn2+, Cu2+ or Ca2+ increased AG-b activity. However, Ag+, Hg2+, Fe3+, EDTA and SDS inhibited AG-a and AG-b activities. The main hydrolysates of agarose by AG-a were neoagarotetraose and neoagarohexaose. The main hydrolysates of agarose by AG-b were neoagarooctaose and neoagarohexaose. When the mixture of AG-a and AG-b were used, agarose was mainly degraded into neoagarobiose.
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Argopecten irradiansChlamys farreri ZnCuCdAsPbHgCdZn1.4117.281.241.59HgPbAsCu 2.17 Mu•g -12.48 Mu•g -14 Mu•g -1
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1997200610 1 AsCdCuHgPbZn2.330.0781.410.00360.376.21 g/LPbCd-Cu-Hg-ZnPb-Cu-ZnPb AsCd-Cu-Pb-ZnHgAs-Cu-ZnAsCd-Hg-Zn pHPb>As>Hg>Cd>Zn>Cr>CuPbAsCrCu 2 10ZnAsCdCuPbHgZny=0.9524x+0.0034R=0.97y=0.8622x+0.0299R=0.95yZnx199720041010%30%AsCdCuHgPbZn7.171.700.1080.02417.611.650.0240.00818.444.2670.535.73 mg/kgHgy=0.0033x-6.50R=0.75 32060206090209060209020 3. 38.7%77.8%
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Laminaria japonicaSargassum pallidumS.kjellmanianum)s.thunbergii1. M/G1.861.501.221.27= (F_MG))/(F_M * F_G)0.620.130.360.412. Cd-SrM/GCu~(2+)MG-Sr~(2+)Ba~(2+)Cd~(2+)M-3. G-~(26)Cu~(2+)Sr~(2+) -COOHSr~(2+)Cu~(2+)Cu~(2+)Cu~(2+)Ca~(2+)Sr~(2+)4.
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In this study, hemolytic activity of venom from the jellyfish Rhopilema esculentum Kishinouye and some factors affecting it were assayed. The HU50 of R. esculentum full venom (RFV) against chicken erythrocytes was 3.40 mu g/ml and a Hill coefficient value was 1.73 suggesting at least two molecules participated in hemolytic activity. The hemolytic activity of RFV was affected by some chemical and physical factors such as divalent cations, EDTA, (NH4)(2)SO4, pH and temperature. In the presence of Mg2+, Cu2+, Zn2+, Fe2+, Ca2+ ( >= 2 mM), Mn2+ (>= 1 mM), EDTA (>= 2 mM) and (NH4)(2)SO4, the hemolytic activity of RFV was reduced. RFV had strong hemolytic activity at the pH 6-10 and the hemolytic ratios were 0.95-1.19. Hemolytic activity was temperature-sensitive and when RFV was pre-incubated at temperatures over 40 degrees C, it was sharply reduced. (c) 2007 Elsevier Ltd. All rights reserved.
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Using a recently developed technique to extract jellyfish venom from nematocysts, the present study investigated the hemolytic activity of Cyanea nozakii Kishinouye nematocyst venom on chicken erythrocytes. Venom extract caused a significant concentration-dependent hemolytic effect. The extract could retain its activity at -80 degrees C but was unstable when kept at 4 degrees C and -20 degrees C for 2 days. The hemolytic activity was inhibited by heating within the range of 37-100 degrees C. The extract was active over a pH range of 5.0-8.63 and the pH optima for the extract was 7.8. Incubation of the venom with sphingomyelin specially inhibited hemolytic activity by up to 70%. Cu2+ and Mn2+ greatly reduced the hemolytic activity while Mg2+, Sr2+ and Ba2+ produced a relatively low inhibiting effect on the hemolytic activity. Treatment with Ca2+ induced a concentration-dependent increase in the hemolytic activity. In the presence of 5 mM EDTA, all the hemolytic activity was lost, however, the venom containing 1.5 mM EDTA was stable in the long-term storage. PLA(2) activity was also found in the nematocyst venom of C. nozakii. These characteristics provide us a fundamental knowledge in the C. nozakii nematocyst venom which would benefit future research. (C) 2010 Published by Elsevier Ltd.
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6-41290-1CuCuCu2NaKCa2+-SO42-Cl-NZ3Re-05826230Ma-4Z-59.0-6.5RedinaRodiniaFeCu-Cu-ZCuNaKCu
