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  • circular dichroism  (2)
  • Chelating Agents metabolism  (1)
  • 1
    Online Resource
    Online Resource
    Metallothioneins and related chelators : Volume 5 (2009)
    Cambridge : Royal Society of Chemistry
    Details Availability
    Keywords: Chelating Agents metabolism ; Heavy metals Toxicology ; Metal ions Physiological effect ; Metallothionein ; Metals, Heavy toxicity ; Metallothionein ; Chelate ; Metallion
    Description / Table of Contents: An essential resource for scientists working in a wide range of disciplines from environmental toxicology and inorganic biochemistry all the way through to physiology and medicine, These sulfur-rich chelators, being important in metal ion homeostasis, find increasing attention. MILS-5, written by 30 internationally recognized experts, focuses on this hot topic. The reader is supported by about 20 tables, more than 80 illustrations and nearly 2000 references. This book is an essential resource for scientists working in a wide range of disciplines from environmental toxicology and inorganic biochemistry all the way through to physiology and medicine
    Type of Medium: Online Resource
    Pages: Online-Ressource (544 p) , 84 b&w, ill
    Edition: RSC eBook Collection 1968-2009
    ISBN: 1847559530 , 9781847559531
    Series Statement: Metal ions in life sciences 5
    URL: http://www.rsc.org/Publishing/eBooks/2009/9781847558992.asp
    URL: https://doi.org/10.1039/9781847559531
    URL: http://www.gbv.de/dms/bowker/toc/9781847559531.pdf
    RVK:
    VH 9750
    Language: English
    Note: Ebook , Chapter 1: METALLOTHIONEINS. HISTORICAL DEVELOPMENT AND OVERVIEW-- Chapter 2: REGULATION OF METALLOTHIONEIN GENE EXPRESSION-- Chapter 3: BACTERIAL METALLOTHIONEINS-- Chapter 4: METALLOTHIONEINS IN YEAST AND FUNGI-- Chapter 5: METALLOTHIONEINS IN PLANTS-- Chapter 6: METALLOTHIONEINS IN DIPTERA-- Chapter 7: EARTHWORM AND NEMATODE METALLOTHIONEINS-- Chapter 8: METALLOTHIONEINS IN AQUATIC ORGANISMS: FISH, CRUSTACEANS, MOLLUSCS, AND ECHINODERMS-- Chapter 9: METAL DETOXIFICATION IN FRESHWATER ANIMALS. ROLES OF METALLOTHIONEINS-- Chapter 10: STRUCTURE AND FUNCTION OF VERTEBRATE METALLOTHIONEINS-- Chapter 11: METALLOTHIONEIN-3, ZINC, AND COPPER IN THE CENTRAL NERVOUS SYSTEM-- Chapter 12: METALLOTHIONEIN TOXICOLOGY: METAL ION TRAFFICKING AND CELLULAR PROTECTION-- Chapter 13: METALLTHIONEIN IN INORGANIC CARCINOGENESIS-- Chapter 14: THIOREDOXINS AND GLUTAREDOXINS. FUNCTIONS AND METAL ION INTERACTIONS-- Chapter 15: METAL ION-BINDING PROPERTIES OF PHYTOCHELATINS AND RELATED LIGANDS.
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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
    Copper-release from yeast Cu(I)-thionein by hypothiocyanite (OSCN−) (1996)
    Springer
    BioMetals 9 (1996), S. 345-349 
    Details
    ISSN: 1572-8773
    Keywords: circular dichroism ; copper-release ; Cu(I)-thionein ; fluorescence ; oxidative burst ; pseudo halides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In the course of an oxidative burst oxygen free radicals and hypothiocyanite (OSCN−), a transiently abundant derivative of thiocyanate (SCN−), are formed in the presence of activated polymorphonuclear leukocytes (PMNs). At the same time Cu(I)-thionein is present and the question arose whether or not thiocyanate and its oxidized form may transiently release highly Fenton active copper to improve the efficacy of the above mentioned oxidative burst. Thus, the reaction of yeast Cu-thionein with OSCN− was examined. Indeed, a release of copper from the Cu(I)-thiolate clusters of the protein was observed ex vivo. Both the chiroptic and luminescence emission signals of Cu-thionein essentially levelled off in the presence of a 15-fold molar excess of OSCN− expressed per equivalent of thionein-copper. The effective copper-releasing activity of this reagent was confirmed by equilibrium dialysis. The demetallized protein could be reconstituted under reductive conditions. SCN− did not affect the copper-thiolate bonding. It rather acts as a potent metabolic source for the transient copper release from Cu-thionein in the presence of activated PMNs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00140603
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