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  • Articles  (31)
  • Springer  (26)
  • De Gruyter  (5)
  • Taylor & Francis
  • 1980-1984  (25)
  • 1945-1949  (4)
  • 1925-1929  (2)
  • Chemistry and Pharmacology  (31)
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  • Articles  (31)
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  • 1
    ISSN: 1432-2234
    Keywords: Closed-shell INDO-CI method ; Trisdiimine iron(II) complexes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An INDO-CI method in π-approximation extended for transition metal complexes with organic ligands is presented. The σ-polarization in the complex is estimated using a two-dimensional EHT calculation and considered in the π-calculation by means of the diagonal Fock matrix elements. The method is tested for four trisdiimine iron(II) complexes. In agreement with the experimental absorption spectra the calculations show that diimine complexes with non-heterocyclicly bound nitrogen atoms exhibit a large red-shift of the characteristic charge-transfer transition increasing the number of aromatic rings. Contrarily, for diimine complexes with heterocyclicly bound nitrogen atoms no shift of the charge-transfer transition was obtained.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1424
    Keywords: Na−K ATPase ; ouabain ; Xenopus ; oocyte ; maturation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary During progesterone-stimulated maturation of defolliculated full-grownXenopus oocytes, the activities of the transport systems forl-alanine, thymidine, chloride, phosphate, and alkali ions decrease. Differences of the extent and time course of these changes suggest that they are controlled by at least partially independent mechanisms. A closer investigation of the Na-K ATPase has shown that in unstimulated oocytes, ouabain produces maximal inhibition when 8–12×109 molecules are bound per cell. This number is bound during the first phase of a diphasic uptake process. Since this phase can be suppressed by increasing the concentration of external K+ to 45 mmol/liter or more, it is concluded that it refers to binding to the Na−K pump in the plasma membrane. Ouabain bound prior to progesterone-induced germinal vesicle breakdown (GVBD) remains bound after the breakdown, although the Na−K pump loses the capacity to bind ouabain after GVBD in oocytes that had not been exposed to ouabain preceding GVBD. In the presence of Mg++ membranes isolated before regulatory inhibition of pumping and ouabain binding show a Na+-dependent incorporation of32P from γ-[32P]-ATP that can be reversed by the addition of K+. The phosphorylation site migrates on LiDS-polyacrylamide gel electropherograms at about 98,000 daltons and can be identified as a Commassie blue-stainable band.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1424
    Keywords: Xenopus ; oocyte ; cotransport ; alanine flux ; sodium flux ; sodium current
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The sodium-dependentl-alanine transport across the plasma membrane of oocytes ofXenopus laevis was studied by means of [14C]-l-alanine,22Na+ and electrophysiological measurements. At fixed sodium concentrations, the dependence of alanine transport on alanine concentration follows Michaelis-Menten kinetics; at fixed alanine concentrations, the transport varies with sodium concentration with a Hill coefficient of 2. In the presence of sodium the uptake of alanine is accompanied by a depolarization of the membrane. Under voltage-clamp conditions this depolarization can be compensated by an inward-directed current. Assuming that this current is carried by sodium we arrive at a 2∶1 stoichiometry for the sodium-alanine cotransport. The assumption was confirmed by direct measurements of both sodium and alanine fluxes at saturating concentrations of the two substrates, which also yielded a stoichiometry close to 2∶1. The sodium-l-alanine cotransport is neither inhibited by furosemide (0.5 mmol/liter) nor by N-methyl amino isobutyric acid (5 mmol/liter). A 20-fold excess ofd-alanine overl-alanine caused about 60% inhibition.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 15 (1927), S. 972-972 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 35 (1948), S. 221-221 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 34 (1947), S. 213-214 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 13 (1980), S. 516-516 
    ISSN: 1612-1112
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 18 (1984), S. 287-293 
    ISSN: 1612-1112
    Keywords: Glass capillary GC-MS ; Chiral stationary phases ; Thio-amino acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Methyl esters of the pentafluoropropionyl-amino acid derivatives of the tetrafunctional, sulphur-bridged, stereoisomeric lanthionines, cystathionines and β-methyl-lanthionines were resolved on glass capillaries coated with the chiral stationary phase N-propionyl-L-valine-N-tert-butylamide-polysiloxane (Chirasil-Val) within 35min. Interestingly, L-cystathionine elutes before its D-enantiomer in contrast to the usual order of emergence on an L-phase. The method was applied to the polypeptide antibiotic nisin, which contains mesolanthionine and 2S,3S,6R-3-methyl-lanthionine. N-Pentafluoropropionyl-S-alkylthiocysteine methyl esters (R=methyl, ethyl, n- and iso-propyl, n- and sec-butyl, n-octyl, neo-pentyl, cyclohexyl-, benzyl-, tolyl-) were separated on Chirasil-Val within 30min. The identity of all derivatives was shown by combined gas chromatography-mass spectrometry.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 12 (1980), S. 233-247 
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Heart mitochondria swollen passively in nitrate salts contract in a respiration-dependent reaction which can be attributed to an endogenous cation/H+ exchange component (or components). The rate of contraction increases with increased extent of passive swelling in both Na+ and K+ salts. Since nearly constant internal cation concentrations are maintained during osmotic swelling, this result suggests that both Na+/H+ and K+/H+ exchange is enhanced by increased matrix volume. Endogenous Mg2+ is also lost with increased matrix volume, and this observation, in conjunction with other evidence available in the literature, suggests that monovalent cation/H+ exchanges may be regulated by divalent cations. Passive exchange of Na+/K+,42K+/K+, and24Na+/Na+ can be readily demonstrated in mitochondria swollen in nitrate. All these exchanges are low or not detectable in unswollen control mitochondria, and it appears that they are manifestations of the activated cation/H+ component (or components) functioning in the absence of ΔpH.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 16 (1984), S. 379-390 
    ISSN: 1573-6881
    Keywords: Quinine ; quinacrine ; mitochondrial K+/H+ antiport ; swelling and contraction of heart mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Quinine inhibits the respiration-dependent extrusion of K+ from Mg2+-depleted heart mitochondria and the passive osmotic swelling of these mitochondria in K+ and Na+ acetate at alkaline pH. These observations concur with those of Nakashima and Garlid (J. Biol. Chem. 257, 9252, 1982) using rat liver mitochondria. Quinine also inhibits the respiration-dependent contraction of heart mitochondria swollen passively in Na+ or K+ nitrate and the increment of elevated respiration associated with the extrusion of ions from these mitochondria. Quinine, at concentrations up to 0.5 mM, inhibits the respiration-dependent42K+/K+ exchange seen in the presence of mersalyl, but higher levels of the drug produce increased membrane permeability and net K+ loss from the matrix. These results are all consistent with an inhibition of the putative mitochondrial K+/H+ antiport by quinine. However, quinine has other effects on the mitochondrial membrane, and possible alternatives to this interpretation are discussed.
    Type of Medium: Electronic Resource
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