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  • 1
    Electronic Resource
    Electronic Resource
    The variability of patterns of sexual dimorphism in the hominoid skull (1990)
    Springer
    Cellular and molecular life sciences 46 (1990), S. 670-672 
    Details
    ISSN: 1420-9071
    Keywords: Hominoids ; crania ; sexual dimorphism ; discriminant analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Univariate and multivariate statistical analyses are applied to a number of cranial dimensions and angles from living hominoids in order to investigate the patterns of sexual dimorphism in these groups. Clear differences in patterns of cranial sexual dimorphisms are demonstrated not only between genera but also within a single species (Homo). These differences overlay the common finding of a sexual size difference in all groups. The results imply that caution is required in using the sexual dimorphisms of living hominoids as models for those anticipated in fossils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01939929
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  • 2
    Electronic Resource
    Electronic Resource
    Electric Fields in Perfused Nerves (1967)
    [s.l.] : Nature Publishing Group
    Nature 214 (1967), S. 393-394 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The resting membrane is permeable to more than one ion6. The potential difference across the membrane is therefore not an equilibrium potential difference. In the steady (resting) state active transport prevents the fluxes through the membrane from changing the compositions of the internal and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/214393a0
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  • 3
    Electronic Resource
    Electronic Resource
    Conformations of P2 Protein of Peripheral Nerve Myelin by Nuclear Magnetic Resonance Spectroscopy (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: High-resolution 1H NMR spectra of P2 protein from bovine peripheral nerve myelin indicate that the protein contains a high degree of tertiary structure in aqueous solution. Denaturation of the protein in urea solutions is a multi-step process. Binding of lysophosphatidylcholine micelles to the protein causes a conformational change and a broadening of NMR peaks from side chains of aromatic amino acid and methionine residues, with much less effect on upfield methyl resonances.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb10830.x
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  • 4
    Electronic Resource
    Electronic Resource
    Infrared dielectric constant of cubic SiC (1995)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 78 (1995), S. 7255-7258 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The real dielectric constant for chemical vapor deposition 3C-SiC grown on silicon (Si) has been determined at 300 K and at 5 K from an analytic fit to interference fringes in transmission over the spectral range from the near infrared to the submillimeter region. This technique is capable of high accuracy being limited typically by the sample thickness and accuracy with which the thickness is measured. The resulting real dielectric constant is lower than the values usually attributed to this material. We find: at 300 K ε 0=9.52 and ε ∞=6.38; at 5 K ε0=9.28 and ε ∞=6.22. In all cases the estimated error is ±0.8%. The observed ratio ε0 /ε∞ agrees with the Lyddane–Sachs–Teller relation to 0.1% at 300 K and 0.2% at 5 K. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.360438
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  • 5
    Electronic Resource
    Electronic Resource
    Erratum: Infrared dielectric constant of gallium arsenide [J. Appl. Phys. 80, 6939 (1996)] (1997)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 81 (1997), S. 3732-3732 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.365497
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  • 6
    Electronic Resource
    Electronic Resource
    Infrared dielectric constant of gallium arsenide (1996)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 80 (1996), S. 6939-6942 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The real dielectric constant of gallium arsenide has been determined at 300 and at 5 K from fits to observed interference in transmission of thin samples with parallel surfaces. Measurement was carried out over all or part of the range 30–4000 cm−1. An accuracy of ±0.5% is estimated based on the quality of the analytic fits and the sample thickness measurement technique. We find at 300 K, ε0=12.90 and ε∞=10.86. At 5 K, ε0=12.46 and ε∞=10.58. An analytic expression for the dielectric function is given which allows accurate values of the real dielectric constant to be determined throughout most of the 0–4000 cm−1 spectral range. The observed ratio ε0/ε∞ agrees with the Lyddane–Sachs–Teller relation calculated with Raman values of transverse and longitudinal optical phonon frequencies to better than 0.1% at 300 and at 5 K. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.363818
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  • 7
    Electronic Resource
    Electronic Resource
    SYNTHESIS AND DEGRADATION OF PROTEIN OF VISUAL RECEPTOR MEMBRANES IN LATERAL EYES OF LIMULUS (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 26 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —The spatial and temporal distribution of labelled protein in lateral eyes of Limulus polyphemus has been followed after injection of l-[3H]leucine into the pericardial sinus. Labelled protein in the eyes rises for 3 h, for the first hour more rapidly in the cytoplasm but thereafter preferentially in the rhabdomal membranes of the visual receptor cells. In light, the label in the membrane reaches a peak at 3 h whereas in dark the peak is at 6 h. The subsequent decrease in label in light has a half life of about 2 h, but in dark is biphasic with halflives of 2 h and 8 days. These results can be interpreted on the basis that the major labelled protein in the rhabdomal membrane is rhodopsin, the degradation rate of which is enhanced when the membranes are depolarized by light.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb04477.x
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  • 8
    Electronic Resource
    Electronic Resource
    ISOLATION AND PARTIAL CHARACTERIZATION OF RAT BRAIN SYNAPTIC PLASMA MEMBRANES (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Synaptic plasma membranes from the cortices of adult rat brain were isolated from synaptosomes prepared by flotation of a washed mitochondrial pellet (P2) in a discontinuous Ficoll-sucrose gradient. Contamination of the synaptosome fraction by microsomes was estimated by enzymic and chemical analysis to be less than 15 per cent. (2) The purified synaptosome fraction was subjected to osmotic shock, subfractionated on a discontinuous sucrose gradient and the distribution of enzymic and chemical markers for synaptic plasma membranes, microsomal membranes and mitochondria was determined. (3) Comparison of synaptosome subfractions prepared in the presence and absence of 1 mM NaH2 PO4/0.1 mM EDTA buffer pH 7.5, indicated that the ionic composition of the isolation medium markedly affected the distribution and enzymic composition of the subfractions. (4) Synaptic plasma membranes prepared in the presence of PO4/EDTA exhibited a 10-fold enrichment in [Na++ K+] ATPase and were characterized by less than 15 and 10 per cent contamination by microsomes and mitochondria respectively. (5) The polypeptide composition of the purified synaptic plasma membranes was compared with the microsomes and mitochondria by polyacrylamide gel electrophoresis in sodium dodecyl sulphate. No differences between the protein and glycoprotein composition of the synaptic plasma membranes and microsomes were detected. The mitochondria, in contrast, possessed a unique protein composition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb11591.x
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  • 9
    Electronic Resource
    Electronic Resource
    STUDIES ON THE LABELLING PATTERNS OF RNA FROM CEREBRAL CORTEX NUCLEI (1969)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 16 (1969), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: RNA labelling patterns in nuclei from rat cerebral cortex were investigated subsequent to intracerebral injection of [3H]uridine. Although there was a rapid uptake of label into the ‘heavy’ regions when nuclear RNA was analysed in density gradients, it was not possible to show conclusive evidence for 455 ribosomal precursor RNA. Methyl-ation of 18S and 28S nuclear RNA became evident only after 2 hr and did not appear to involve the intermediacy of RNA species of higher molecular weight.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1969.tb08989.x
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  • 10
    Electronic Resource
    Electronic Resource
    THE HALF-LIFE OF ACETYLCHOLINESTERASE IN MATURE RAT BRAIN (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —The rate of degradation of acetylcholinesterase [EC 3.1.1.7] in mature rat cerebral cortex was determined from the time course of the label introduced into the protein by one intraventricular injection of l-leucine-l-14C. The half life of the enzyme was 2.84 ± 013 days.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb04319.x
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