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  • 1
    Electronic Resource
    Electronic Resource
    Circular dichroism, luminescence, and electronic absorption of copper binding sites in metallothionein and its chemically synthesized .alpha. and .beta. domains (1992)
    s.l. : American Chemical Society
    Inorganic chemistry 31 (1992), S. 5526-5533 
    Details
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ic00052a031
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  • 2
    Electronic Resource
    Electronic Resource
    Analogous copper(I) coordination in metallothionein from yeast and the separate domains of the mammalian protein (1992)
    Springer
    BioMetals 5 (1992), S. 187-191 
    Details
    ISSN: 1572-8773
    Keywords: circular dichroism ; copper-thiolate cluster ; fluorescence ; metallothionein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The three-dimensional structures of both vertebrate Cu12-metallothionein (class 1) and yeast Cu8-thionein (class 2) are still unknown. The different copper:protein stoichiometry compared with that of the (ZnCd)7-metallothioneins was expected to alter the metal-thiolate cluster structure considerably. In order to avoid possible domain interactions in the hepatic rat metallothionein, separate chemically synthesized α-and β-domains were used rather than the apoprotein. Apo yeast thionein, and the α-and β-domains of rat liver metallothionein-2 were reconstituted by Cu(I) titration. Reconstitution steps were monitored using spectroscopic methods including luminescence emission and circular dichroism. Upon UV irradiation a linear increase in intensity of the orange-red luminescence was observed near 600 nm up to 6 Cu eq using either compound regardless of the different cysteine sulfur content (yeast thionein 12S, α-domain 11S, β-domain 9S). The characteristic dichroic properties of the yeast copper-protein between 240 and 400 nm were in good agreement with those of the respective class 1 metallothionein domains. All observed Cotton bands were of similar shape and appeared in the same wavelength regions. However, the molar ellipticities were less pronounced in the α-and β-fragments employed. There appears to be a striking similarity between the oligonuclear Cu(I) binding centers in all metallothionein species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01061327
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  • 3
    Electronic Resource
    Electronic Resource
    Intestinal administration of copper and its transient release into venous rat blood serum concomitantly with metallothionein (1993)
    Springer
    BioMetals 6 (1993), S. 115-118 
    Details
    ISSN: 1572-8773
    Keywords: copper transport ; metallothionein ; metallothionein-immunoreactivity ; portal serum ; rat jejunum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The molecular side of copper transport in biological systems is unknown. It was attempted to examine the copper and metallothionein (MT) release into the portal blood in rats in vivo. After direct administration of Cu(II) into the jejunum the copper and MT levels were distinctively higher in the portal venous serum compared with that of the vena cava inferior. MT in gel filtrated serum samples was analyzed immunologically employing ELISA and a monoclonal antibody to rat MT-I. Affinity chromatography on Protein A-Sepharose resulted in a higher immunoreactivity in the portal compartment as deduced from an elevated MT-antibody complex. It is assumed that MT serves as a genuine transport system for cuprous copper during the mucosal-to-serosal flux of this biologically important transition metal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00140112
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  • 4
    Electronic Resource
    Electronic Resource
    Pulse radiolytically determined superoxide dismutase mimicking activity of copper-putrescine-pyridine, a diSchiff base coordinated copper complex (1993)
    Springer
    BioMetals 6 (1993), S. 11-15 
    Details
    ISSN: 1572-8773
    Keywords: diSchiff base Cu-SOD mimetic copper complexes ; hyperthermia ; pulse radiolysis ; reactive oxygen species (ROS)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In order to exclude possible interferences in the many indirect superoxide dismutase (SOD) activity measurements using the copper-putrescine-pyridine complex (Cu-PuPy) a pulse radiolytic study on this diSchiff base copper complex has been devised and sucessfully performed. The reaction kinetics and rate constants of pulse radiolytically generated superoxide in the presence of Cu-PuPy reveal pseudo first-order characteristics. The rate constant (k 2 = 6 ± 1 × 108 m −1 s −1) is comparable to that of an Fe-SOD and is approximately a factor of 3 lower than that of bovine Cu2Zn2-SOD. The superoxide dismutating activity of Cu-PuPy shows a more pronounced temperature dependence compared with that of Cu2Zn2-SOD. Arrhenius analyses yielded activation energies of 7.8 ±0.3 and 4.6 ± 0.2 kcal mol−1 for Cu-PuPy and Cu2Zn2-SOD, respectively. The rate constant of the reaction of superoxide and Cu-PuPy is highest at pH 5.0. The possible application of Cu-PuPy for new therapeutic strategies on all types of inflammatory diseases appears to be promising.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00154227
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  • 5
    Electronic Resource
    Electronic Resource
    Copper transfer through the intestinal wall Serosal release of metallothionein (1990)
    Springer
    BioMetals 3 (1990), S. 141-145 
    Details
    ISSN: 1572-8773
    Keywords: Copper transfer ; Metallothionein ; Mammalian intestine ; ELISA ; Immunoblotting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The elucidation of the molecular side of copper transport in biological systems is a promising task. In this context the transfer of ingested copper into the portal blood plasma was examined. Intralumenal addition of 200 μM copper caused the release of Cu-thionein into the venous effluent. This Cu-thionein became detectable after prior perfusion of the porcine small bowel using a modified isotonic phosphate-buffered saline (Pi/NaCl) medium. The protein was characterized by gel chromatography, luminescence, electronic absorption and immunological identification. ELISA and immunoblotting employing a murine monoclonal antibody to rat liver metallothionein-I proved to be most convenient. Using buffer-loaded sacs of porcine jejunum into which Cu2+, Zn2+ and Cd2+ were added, the release of metallothionein into the serosal fluid was successfully seen by ELISA. The observed excretion of metallothionein into the portal compartment may be a genuine metal transport system for many biochemically active metals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01179524
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  • 6
    Electronic Resource
    Electronic Resource
    Inhibition of 3 H-Thymidine Incorporation into Rat Liver Nuclei by E. coli L -Asparaginase (1970)
    [s.l.] : Nature Publishing Group
    Nature 225 (1970), S. 652-653 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The methods used in this study-with a few modifications-have been described911. Female Wistar rats with an average initial weight of 90 g have been used throughout this study. E. coli L-asparaginase (220 IU/mg protein, crystal suspension in 3.5 M (NH4)2SO4) was a gift from Boehringer, Mannheim. The ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/225652a0
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  • 7
    Electronic Resource
    Electronic Resource
    Reactivity of active center analogs of Cu2Zn2 superoxide dismutase on activated polymorphonuclear leukocytes (1990)
    Springer
    Inflammation 14 (1990), S. 409-419 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In unseparated human blood the Cu2Zn2 superoxide dismutase mimetic reactivity of several differently coordinated low Mr copper chelates on TPA-activated polymorphonuclear leukocytes was evaluated and compared to their apo-chelates, CuSO4, and the native enzyme. Similar to intact superoxide dismutase, 350–400 nM Cu flexibly complexed in a di-Schiff base mode in CuPu(Py)2 and CuPu(Im)2, respectively, was sufficient to inhibit the oxidative burst-dependent superoxide production of human blood phagocytes by 50%. Acetate-or biuret-type copper chelates behaved like CuSO2. The catalytic superoxide dismuting reactivity of the di-Schiff base active center analogs of SOD was confirmed using isolated porcine PMNs. Even in the presence of 600μM albumin as a model for competitive copper chelation in biological fluids CuPu(Py)2 and CuPu(Im)2 remained active. The stability during the Cu(I)/Cu(II) redox cycling was demonstrated in the presence of activated PMNs and albumin, taking advantage of the electron paramagnetic properties of CuPu(Py)2 and CuPu(Im)2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00914092
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  • 8
    Electronic Resource
    Electronic Resource
    Antiinflammatory reactivity of copper(I)-thionein (1990)
    Springer
    Inflammation 14 (1990), S. 471-483 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In unseparated human blood the reactivity of yeast copper (I)-thionein on TPA-activated polymorphonuclear leukocytes was evaluated and compared with low Mr copper chelates exerting Cu2Zn2 superoxide dismutase mimetic activity. Cu, 18ΜM, in the form of Cu-thionein was sufficient to inhibit the Superoxide production of activated human blood phagocytes by 50%. Furthermore, the scavenging of hydroxyl radicals and singlet oxygen by Cu(I)-thionein was determined, using the 2-deoxyribose fragmentation assay induced by decaying K3CrO8 and the NADPH oxidation caused by UVA illuminated psoralen, respectively. The inhibitory reactivity of Cu-thionein in both assays was compared with that of serum proteins including albumin, ceruloplasmin, transferrin, and ferritin. The galactosamine/endotoxininduced hepatitis in male NMRI mice was used to evaluate the antiinflammatory reactivity of Cu-thionein in vivo. The serum copper, superoxide dismutase, and sorbitol dehydrogenase concentrations, as well as the activity of polymorphonuclear leukocytes in unseparated blood seemed most appropriate to quantify the protective capacity of Cu-thionein in the course of an oxidative stress-dependent liver injury. The intraperitoneal application of 32.5 Μmol/kg thionein-Cu limited this damage to 45%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00914269
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  • 9
    Electronic Resource
    Electronic Resource
    Erythrocuprein (1971)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 83 (1971), S. 939-940 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.1971083221193
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