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  • 1
    Electronic Resource
    Electronic Resource
    Static and dynamic hyperfine coupling of FE(II) in the FeS4 unit. Results of Mössbauer spectroscopy on a [P(C6H5)4]2[Fe(SC6H5)4] monocrystal (1988)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 89 (1988), S. 732-740 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The hyperfine coupling parameters of Fe(II) in the FeS4 unit of the complex anion [Fe(SC6H5)4]2− have been determined from an analysis of Mössbauer spectra of a monocrystal in the temperature range of 1.5 to 20 K and in magnetic fields of 0 to 6.7 T. Dynamic spin fluctuation effects have been included in the analysis by a stochastic model with spin–lattice relaxation. Anisotropy in the relaxation matrix element was of moderate significance and apparent only at low fields. The use of a monocrystal allows more precise determination of hyperfine parameters, because it avoids the averaging procedures which are inherent in studies on polycrystalline material. The set of parameters is essentially identical with that reported for reduced rubredoxin and indicates that the electronic ground state of [Fe(SC6H5)4]2−, predominantly of [3z2−r2] character, simulates very well the ground state of the protein FeS core.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.455196
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  • 2
    Electronic Resource
    Electronic Resource
    Exchange interactions, charge delocalization, and spin relaxation in a mixed-valence di-iron complex studied by Mössbauer spectroscopy (1993)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 99 (1993), S. 6421-6428 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Exchange interactions and charge transfer in the Fe2+Fe3+ pair of the mixed valence [Fe2S2(dimethylmethanebisbenzimidazolate)2]3− trianion have been studied by analysis of Mössbauer spectra in the temperature range of 1.5–180 K and in applied fields of 10 mT, 0.35 T, and 6.2 T. The low-temperature spectra reveal a ground state with total spin St=1/2 and hyperfine parameters intermediate between values for a Fe2+Fe3+ localized mixed-valence pair and a fully delocalized system where the two iron atoms are equivalent. A consistent set of hyperfine parameters has been derived by fitting the spectra with a stochastic relaxation model taking into account spin relaxation in the St=1/2 state and electron hopping between the iron ions. An interpretation of the values of the hyperfine parameters has been given by solving a spin Hamiltonian, which includes antiferromagnetic and double exchange in an asymmetric Fe2+Fe3+ pair and which allows partial electron delocalization. Using the value a2=0.8 for the delocalization coefficient and an estimate of Δ=105 cm−1 for the difference between the St=1/2 and the first excited St=3/2 state we have derived limits for the exchange-coupling constant J, the double-exchange parameter B, and the energy difference EA−EB arising from the two possible configurations FeA2+FeB3+ and FeA3+FeB2+, i.e., 70 cm−1(approximately-less-than)J(approximately-less-than)300 cm−1, 0〈||B||(approximately-less-than)395 cm−1, and 0〈||EA−EB||(approximately-less-than)590 cm−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.465881
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  • 3
    Electronic Resource
    Electronic Resource
    Glycoprotein III (Clusterin, Sulfated Glycoprotein 2) in Endocrine, Nervous, and Other Tissues: Immunochemical Characterization, Subcellular Localization, and Regulation of Biosynthesis (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 61 (1993), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Specific antisera were raised against the A and B chains of glycoprotein III. lmmunoblotting revealed that in adrenal medulla both chains migrate very closely together in two-dimensional electrophoresis. Both chains with slightly differing molecular sizes are found in several endocrine tissues and in brain, kidney, liver, and serum. The mRNA has an analogous widespread distribution. In primary cultures of chromaffin cells the level of message becomes significantly increased by treatment with hista-mine or 12-O-tetradecanoylphorbol 13-acetate/forskoIin. However, the increase is small when compared with that of secretogranin II. The subcellular localization of glycoprotein III in endocrine organs and in the posterior pituitary was investigated by subcellular fractionation and immuno-electron microscopy. Glycoprotein III was found to be confined to the large densecore vesicles of these organs. For a discussion of the function of glycoprotein III, its localization in these organelles has to be taken into account.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1993.tb13645.x
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  • 4
    Electronic Resource
    Electronic Resource
    Biogenesis of Chromaffin Granules: Incorporation of Sulfate into Chromogranin B and into a Proteoglycan (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 45 (1985), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The incorporation of [35S]sulfate into the soluble proteins of chromaffin granules was studied. Isolated bovine chromaffin cells were pulse-labeled with [35S]sulfate. The radioactively labeled products were characterized by one- and two-dimensional electrophoresis. Three proteins of chromaffin granules were preferentially labeled. One was identified by immunoprecipitation as chromogranin B (Mr 100,000). This result explains why during cellular synthesis the chromogranin B precursor is converted into a significantly more acidic protein. During chase periods, the newly synthesized chromogranin B was progressively degraded by endogenous proteases. A second labeled protein. much less labeled than chromogranin B, was identified as chromogranin A. The largest portion of the radioactive label was found in a heterogeneous component (Mr 86,000 100,000; pI 4.3–5.0). Digestion experiments with chondroitinase ABC demonstrated that this labeled component and a comigrating Coomassie Blue-stained spot were selectively degraded by this enzyme. This establishes that this component is a proteoglycan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb07215.x
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  • 5
    Electronic Resource
    Electronic Resource
    Dynamic conversion of optical modes in magnetic garnet films induced by resonances of periodic stripe domains (1994)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 76 (1994), S. 3272-3278 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Magnetic garnet films of composition (Y,Bi)3(Fe,Al)5O12 are grown by liquid phase epitaxy on [111] oriented substrates of Gd3Ga5O12. They support periodic lattices of parallel stripe domains. A simple strip antenna is used to excite the domain wall resonance and the two branches of the domain resonance in the frequency range up to 5 GHz. The resonance frequencies and the dynamic components of the magnetization are calculated using a hybridization model. Good agreement between calculated and measured resonance frequencies is obtained if the quality factor of the film is larger than 0.6. Optical modes are coupled into the waveguiding film. The excited domain resonances cause dynamic conversion of transverse electric and transverse magnetic modes by the Faraday and the Cotton–Mouton effects. Mode coupling and conversion are calculated by the perturbation theory. The dynamic conversion efficiencies are measured at the fundamental and the first harmonic frequency and at zero diffraction order as a function of the static induction applied in the film plane parallel to the stripes. Conversion efficiencies up to 18% are achieved at a frequency of 2.8 GHz. From the experimental data the precession angles are derived.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.357448
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  • 6
    Electronic Resource
    Electronic Resource
    UPTAKE OF CALCIUM BY CHROMAFFIN GRANULES IN VITRO (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 28 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Partly purified chromaffin granules were incubated in vitro with Ca2+ (with trace amounts of 45Ca2+) in concentrations ranging from 4 μm to 1 mm. After incubation the granules were washed with media containing EDTA and then subjected to density gradient centrifugation (1.3 to 2.0 m-sucrose solutions) in order to characterize the particles which had taken up 45Ca2+. By using marker enzymes and various inhibitors of Ca2+ uptake into such cell particles as mitochondria it was established that under the conditions of the experiments chromaffin granules took up Ca2+ from the incubation medium. To characterize this uptake a simplified density gradient procedure was tested and found to be suitable. The uptake of Ca2+ into chromaffin granules was strongly dependent on temperature. It was not activated by ATP. The uptake was linear up to 10 min. At high calcium concentrations (above 200 μm) the rate of uptake levelled off. The uptake at 37°C was 1 nmol Ca2+/mg protein/min at a Ca2+ concentration of 500 μm. Mg2+ had no influence on Ca2+ uptake, whereas Sr2+ (1 mm) inhibited it. The methods established in this study should prove useful for a further characterization of this Ca2+ uptake into chromaffin granules which is likely to represent a useful model for the Ca2+ uptake occurring in the intact gland.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10419.x
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  • 7
    Electronic Resource
    Electronic Resource
    Accumulation of [3H]ATP in small dense core vesicles of superfused vasa deferentia (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 33 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb05227.x
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  • 8
    Electronic Resource
    Electronic Resource
    The arrangement of dopamine β-hydroxylase (EC 1.14.2.1) and chromomembrin B in the membrane of chromaffin granules (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb02642.x
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  • 9
    Electronic Resource
    Electronic Resource
    Increased specific activity of membrane-bound dopamine β-hydroxylase in chromaffin granules after reserpine treatment (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 28 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10638.x
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  • 10
    Electronic Resource
    Electronic Resource
    CHARACTERIZATION AND TOPOGRAPHY OF THE GLYCOPROTEINS OF ADRENAL CHROMAFFIN GRANULES (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The glycoproteins of the membranes of bovine chromaffin granules were characterized by two polyacrylamide gel electrophoresis systems. Five components (I-V) were demonstrated with apparent molecular weights ranging in the unreduced form from 45,000 to 150,000. Glycoprotein I was identified as the enzyme dopamine β-hydroxylase. Four of these glycoproteins (with the exception of component IV) were apparently also present in the membranes of pig and horse chromaffin granules. The soluble proteins of chromaffin granules contained at least three glycoproteins. Only glycoprotein I (dopamine β-hydroxylase) was present both in the soluble content and in the membranes of chromaffin granules. Affinity chromatography with lectins demonstrated that from the soluble proteins only dopamine β-hydroxylase was adsorbed by concanavalin A, whereas none of these proteins reacted with wheat germ lectin and Ricinus communis agglutinin. Three membrane proteins including dopamine β-hydroxylase and glycoprotein II as major components were adsorbed by concanavalin A, whereas wheat germ lectin bound only component II and a small amount of component III. By electron microscopy it was demonstrated that concanavalin A did not bind to intact chromaffin granules whereas ruthenium red and cationized ferritin did. Isotope labelling after galactose oxidase treatment revealed that at least the carbohydrate portion of the major glycoproteins is present on the inner side of the granule membranes facing the content.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb04507.x
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