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  • 1985-1989  (5)
  • 1989  (5)
  • Polymer and Materials Science  (3)
  • binding  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 461-470 
    ISSN: 1573-6881
    Keywords: Mitochondria ; hexokinase ; binding ; receptor ; VDAC ; porin ; DCCD ; sequence homology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The outer mitochondrial membrane receptor for hexokinase binding has been identified as the VDAC protein, also known as mitochondrial porin. The ability of the receptor to bind hexokinase is inhibited by pretreatment with dicyclohexylcarbodiimide (DCCD). At low concentrations, DCCD inhibits hexokinase binding by covalently labeling the VDAC protein, with no apparent effect on VDAC channel-forming activity. The stoichiometry of [14C]-DCCD labeling is consistent with one to two high-affinity DCCD-binding sites per VDAC monomer. A comparison between the sequence of yeast VDAC and a conserved sequence found at DCCD-binding sites of several membrane proteins showed two sites where the yeast VDAC amino acid sequence appears to be very similar to the conserved DCCD-binding sequence. Both of these sites are located near the C-terminal end of yeast VDAC (residues 257–265 and 275–283). These results are consistent with a model in which the C-terminal end of VDAC is involved in binding to the N-terminal end of hexokinase.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 28 (1989), S. 1475-1484 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: By use of agarose gel electrophoresis, the sieving of spherical particles in agarose gels has been quantitated and modeled for spheres with a radius (R) between 13.3 and 149 mm. For quantitation, the electrophoretic mobility has been determined as a function of agarose percentage (A). Because a previously used model of sieving [D. Rodbard and A. Chrambach (1970) Proc. Natl. Acad. Sci. USA 65, 970-977] was found incompatible with some of these data, alternative models have been tested. By use of an underivatized agarose, two models, both based on the assumption of a single effective pore radius (PE) for each A, were found to yield PE values that were independent of R and that were in agreement with values of PE obtained independently (PE = 118 nm × A-0.74): sieving by altered hydrodynamics in a cylindrical tube of radius, PE, and sieving by steric exclusion from a circular hole of radius, PE. The same analysis applied to a 6.5% hydroxyethylated commercial agarose yileded a steeper PE vs A plot and also agreement of the above tow models with the data. The PE vs A plot was significantly altered by both further hydroxyethylation and factors that cause variation in the electro-osmosis found in commercial agarose.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1040-0397
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Five crown ethers with four ring oxygen atoms and different types of pendant groups were used to prepare ion-selective electrodes by coating a membrane containing the crown ether on the tip of a silver wire incorporated in a flow cell. A flow injection analysis study was conducted to determine the potentiometric selectivities of the crown ethers for lithium, sodium, potassium, magnesium, and calcium ions. It was found that crown ethers with neutral side arms show selectivities for lithium over other ions, while those of acidic side arms show selectivities for potassium over the other ions. The effect of the addition of trioctylphosphine oxide to the electrode matrix was also investigated. A comparison is made between the potentiometric selectivities of the crown ethers for certain metal ions and their selectivities in extracting the ions into an organic phase.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 27 (1989), S. 1911-1925 
    ISSN: 0887-6266
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Carboxy-terminated polybutadiene neutralized with Cu2+ (CuPBD) and its blend with poly(styrene-co-4-vinylpyridine) (SVP) were examined by differential scanning calorimetry (DSC), transmission electron microscopy (TEM), small-angle x-ray scattering (SAXS), and extended x-ray absorption fine structure (EXAFS) spectroscopy. The DSC results indicate that in the blend substantial mixing occurs in the CuPBD-rich phase, although complete miscibility is not achieved, and the SVP-rich phase remains relatively pure. The TEM micrographs indicate that the morphology, while irregular, is reasonably described as bicontinuous, with a domain size of order 100 nm. The SAXS patterns show that the ionic aggregates present in CuPBD are destroyed upon blending, which is interpreted as being due to steric hindrances between ionic groups coordinated to vinylpyridine nitrogens. The EXAFS radial structure function of the blend exhibits a marked decrease in the Cu-Cu peak in comparison with CuPBD, indicating a change in local structure upon blending. The results indicate that some of the SVP is miscible with CuPBD owing to complexation between the pendant pyridine groups and the Cu2+ ions, which disrupts the ionic aggregates. However, the two materials are not fully miscible, leading to a rather coarse two-phase morphology.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 24 (1989), S. 1-8 
    ISSN: 0148-7280
    Keywords: sperm-zona interaction ; fertilization ; zona pellucida ; receptors ; binding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In mammalian fertilization, sperm bind to the zona pellucida, a glycoprotein matrix forming a shell surrounding the oocyte. Subsequently, one of the bound sperm penetrates the zona and fertilizes the egg. The adhesion between sperm and zona is mediated by complementary receptor-ligand pairs. Recent biochemical evidence has identified likely candidates for these molecules in the mouse. Biophysical studies have predicted that very few (possibly as few as one) bonds are needed to tether a motile sperm to the zona. We have used the data characterizing the putative receptors of the mouse sperm to predict the number of bonds they can form with the zona ligands. Our calculations indicate that few bonds probably form between the sperm and zona during the initial contact when the sperm is captured, supporting the hypothesis that fertilization depends on the action of a very few sperm-zona bonds.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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