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  • Amyloplast  (1)
  • Cu2Pt+IIPt3+IVS8; Copperthioplatinate(II,IV)  (1)
  • Escherichia coli  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Alkaline inorganic pyrophosphatase and starch synthesis in amyloplasts (1986)
    Springer
    Planta 167 (1986), S. 140-145 
    Details
    ISSN: 1432-2048
    Keywords: Alkaline pyrophosphatase ; Amyloplast ; Arum (starch synthesis) ; Glycine (starch synthesis) ; Starch synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The aim of this work was to see if amyloplasts contained inorganic pyrophosphatase. Alkaline pyrophosphatase activity, largely dependant upon MgCl2 but not affected by 100 μM ammonium molybdate or 60–100 mM KCl, was demonstrated in exracts of developing and mature clubs of the spadix of Arum maculatum L. and of suspension cultures of Glycine max L., but not in extracts of the developing bulb of Allium cepa L. The maximum catalytic activity of alkaline pyrophosphatase in the above tissues showed a positive correlation with starch synthesis, and in the first two tissues was shown to exceed the activity of ADPglucose pyrophosphorylase. Of the alkaline pyrophosphatase activity in lysates of protoplasts of suspension cultures of Glycine max, 57% was latent. Density-gradient centrifugation of these lysates showed a close correlation between the distribution of alkaline pyrophosphatase and the plastid marker, nitrite reductase. It is suggested that much, if not all, of the alkaline pyrophosphatase in suspension cultures of Glycine max is located in the plastids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446381
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  • 2
    Electronic Resource
    Electronic Resource
    Colicin M is inactivated during import by its immunity protein (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 388-396 
    Details
    ISSN: 1617-4623
    Keywords: Escherichia coli ; Colicin M ; Immunity ; Periplasm
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Colicin M (Cma) displays a unique activity that interferes with murein and O-antigen biosynthesis through inhibition of lipid-carrier regeneration. Immunity is conferred by a specific immunity protein (Cmi) that inhibits the action of colicin M in the periplasm. The subcellular location of Cmi was determined by constructing hybrid proteins between Cmi and the TEM-β-lactamase (BlaM), which confers resistance to ampicillin only when it is translocated across the cytoplasmic membrane with the aid of Cmi. The smallest Cmi'-BlaM hybrid that conferred resistance to 50 μg/ml ampicillin contained 19 amino acid residues of Cmi; cells expressing Cmi'-BlaM with only five N-terminal Cmi residues were ampicillin sensitive. These results support a model in which the hydrophobic sequence of Cmi comprising residues 3–23 serves to translocate residues 24–117 of Cmi into the periplasm and anchors Cmi to the cytoplasmic membrane. Residues 8–23 are integrated in the cytoplasmic membrane and are not involved in Cma recognition. This model was further tested by replacing residues 1–23 of Cmi by the hydrophobic amino acid sequence 1–42 of the penicillin binding protein 3 (PBP3). In vivo, PBP3'-'Cmi was as active as Cmi, demonstrating that translocation and anchoring of Cmi is not sequence-specific. Substitution of the 23 N-terminal residues of Cmi by the cleavable signal peptide of BlaM resulted in an active BlaM'-'Cmi hybrid protein. The immunity conferred by BlaM'-'Cmi was high, but not as high as that associated with Cmi and PBP3'-'Cmi, demonstrating that soluble Cmi lacking its membrane anchor is still active, but immobilization in the cytoplasmic membrane, the target site of Cma, increases its efficiency. CmiΔ1-23 remained in the cytoplasm and conferred no immunity. We propose that the immunity protein inactivates colicin M in the periplasm before Cma can reach its target in the cytoplasmic membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172531
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  • 3
    Electronic Resource
    Electronic Resource
    Synthese und Kristallstruktur von Cu2PtIIPt3IVS8Professor Heinrich Oppermann zum 60. Geburtstag gewidmet (1994)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 620 (1994), S. 1909-1914 
    Details
    ISSN: 0044-2313
    Keywords: Cu2Pt+IIPt3+IVS8; Copperthioplatinate(II,IV) ; mixed valent compounds ; crystal structure ; Rietveld refinement ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Synthesis and Crystal Structure of Cu2PtIIPt3IVS8(NH4)2PtCl6 and Cu(CH3COO)2 were reacted at 380 K in a constant flow of H2S in the molar ratio of 2:1. Subsequent annealing of the product in sealed quartz glass ampoules in the presence of CuS as a buffer for the sulfur activity (temperature range 770 to 870 K) yields Cu2Pt4S8 as a polycrystalline, greyish black powder. Cu2Pt4S8 crystallizes in the space group P2/n (No. 13) with the cell parameters a = 10.6478(2), b = 6.9350(1), c = 6.7411(1) Å, β = 91.942(1), Z = 2. The structure determination and refinement were performed by the means of x-ray powder diffraction data of this first copperthioplatinate. There are no isotypic compounds known, so far. According to the characteristic coordination of the metals by sulfur, the oxidation states are Cu+I, Pt+II and Pt+IV, the compound may be formulated as Cu2Pt+IIPt3+IVS8. Cu2Pt4S8 exhibits diamagnetic and semiconducting properties.
    Notes: Die Umsetzung von (NH4)2PtCl6 und Cu(CH3COO)2 im molaren Verhältnis von 2:1 bei 380 K im H2S Strom, gefolgt von Tempern des Produktes in abgeschmolzenen Quarzglasampullen zwischen 770 und 870 K, in Gegenwart von CuS als Puffer für die Schwefelaktivität, ergibt Cu2Pt4S8 als polykristallines, grau-schwarzes Pulver. Cu2Pt4S8 kristallisiert in der Raumgruppe P2/n (Nr. 13) mit den Gitterkonstanten a = 10,6478(2), b = 6,9350(2), c = 6,7411(1) Å, β = 91,942(1), Z = 2. Die Strukturaufklärung und -verfeinerung erfolgten unter Verwendung von Röntgenpulverdaten dieses ersten Kupferthioplatinats. Isotype Verbindungen sind nicht bekannt. Nach der jeweils charakteristischen Umgebung durch Schwefel liegen Cu+I, Pt+II und Pt+IV gemäß Cu2Pt+IIPt3+IVS8 vor. Cu2Pt4S8 ist diamagnetisch und halbleitend.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19946201112
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