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  • Electronic Resource  (8)
  • 1985-1989  (4)
  • 1975-1979  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    BJOG 82 (1975), S. 0 
    ISSN: 1471-0528
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A gynandroblastoma of the ovary in a 17-year-old girl is reported. Primary amenorrhoea, hirsuties and slight clitoral enlargement were associated with the tumour and high levels of circulating testosterone were found. This is the first gynandroblastoma in which Reinke crystalloids have been identified in the Leydig cell component. The criteria for the diagnosis of this tumour and its histogenesis are discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 107 (1985), S. 2982-2983 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Cambridge : Cambridge University Press
    Religious studies 15 (1979), S. 582-582 
    ISSN: 0034-4125
    Source: Cambridge Journals Digital Archives
    Topics: Theology and Religious Studies
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 266 (1979), S. 295-310 
    ISSN: 1432-069X
    Keywords: Fibronectin ; Skin ; Basement membranes ; Immunohistochemistry ; Electron microscopy ; Fibronectin ; Haut ; Basalmembran ; Immunohistochemie ; Elektronenmikroskopie
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Die Verteilung des extracellulären Glykoproteins Fibronectin im Haut- und Zungengewebe der Ratte wurde unter Verwendung von spezifischem Antiserum licht- und elektronenmikroskopisch mit Hilfe der Immunofluorescenz- und Immunoperoxidasemethoden untersucht. Aus den Ergebnissen schließen wir, daß Fibronectin weder in stabilen, differenzierten Gewebeteilen wie Talgdrüsen, Matrix, Mark, Rinde oder Cuticula des Haares oder der inneren und äußeren Haarwurzelscheide, noch in Geweben, in denen die Zellen zum Teil beweglich sind (z. B. Epidermis), vorkommt. Es ist aber charakteristisch für Zonen, wo Zellteilung in Berührung mit einem extracellulären Gerüst vor sich geht, wie z. B. an einer Basalmembran oder in lockerem Bindegewebe. Auffallende Beispiele waren die mit Follikelepithelien verbundene Hyalinmembran und Bindegewebsscheide, die unter Gefäßendothelzellen liegende Basalmembran, die Bindegewebe, welche die Nerven- und Muskelfaserbündel umgeben und durchsetzen und das Bindegewebe der Dermis. Im letzteren Falle war das Fibronectin oft mit Kollagenfasern eng verbunden. In der Basalmembran an der Grenze zwischen Dermis und Epidermis war Fibronectin an der Plasmamembran der basalen Zellen und im Gebiet der Lamina lucida zu finden. Es bestand kein Zusammenhang mit spezifischen Stellen der Zellen-Substrat-Adhäsion wie den Hemidesmosomen. Das endoplasmatische Reticulum der Fibroblaste ließ sich stark färben — ein Hinweis, daß diese Zellen einen wichtigen Ort der Synthese darstellen.
    Notes: Summary Specific antiserum was used to investigate the distribution of the extracellular glycoprotein, fibronectin, in rat skin and tongue tissue by light and electron microscopy with immunofluorescence and immunoperoxidase techniques. We conclude that fibronectin is absent from stable, differentiated parts of tissues, such as the sebaceous glands or the matrix, medulla, cortex, and cuticles of the hair and the inner and outer root sheaths, or even in tissues in which there is some cell movement, such as the epidermis. It is, however, characteristic of sites at which cell division is occurring in contact with an extracellular scaffolding, such as basement membrane or loose connective tissue. Conspicuous examples were in the glassy membrane and connective tissue sheath associated with the follicular epithelium, the basement membrane underlying vascular endothelial cells, the connective tissues surrounding and investing nerve and muscle fibre bundles, and the dermal connective tissue where fibronectin was often associated closely with collagen fibres. At the basement membrane of the dermal/epidermal junction, fibronectin occurred at the plasma membrane of the basal cells and in the lamina lucida area. There was no correlation with specific areas of cell-substrate adhesion, such as the hemidesmosomes. The endoplasmic reticulum of fibroblasts stained strongly suggesting that these cells represent a major site of synthesis.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 2301-2332 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Physical studies and conformational analysis of human glycophorin A suggest a revised model for its molecular organization, self-association, and interactions with the erythrocyte membrane. Intrinsic viscosity has been used to study, under more physiological conditions, the monomer-dimer equilibrium demonstrated previously by polyacrylamide-SDS gel electrophoresis. The results show that the equilibrium persists in the absence of detergent and support earlier indications that the dimer is probably the physiologically relevant form and that it is promoted by salt, inhibited by conventional denaturants, and abolished by carboxymethylation.Combined application of CD, fitted to the poly-(L-lysine) model spectra of Greenfield and Fasman, and conformational prediction, by the statistical method of Chou and Fasman and the stereochemical approach of Lim, suggests five helical sequences in glycophorin A: Arg-39 to Tyr-52 (A); Gln-63 to Glu-70 (B); Glu-72 to Leu-89 (C); Ile-95 to Lys-101 (D); and Leu-118 to Asn-125 (E). Sequence A occurs only at low pH and may be stabilized by favorable noncovalent interactions of O-linked tetrasaccharide side chains. The other four helices all occur in the dimeric form of glycophorin A at physiological pH and ionic strength. Sequence D is destroyed by trypsin, and is also lost on conversion to the monomeric form of the glycoprotein at low ionic strength. Sequence E is denatured by 6M guanidine hydrochloride/4M urea. Sequences B and C, which are separated by a single proline residue, are stable under all these conditions.Dimerization of the major, hydrophobic helical sequence, (C) may be promoted and directed by an adjacent short sequence of intermolecular parallel β-sheet (Leu-90 to Tyr-93). It is proposed that these two structures span the lipid bilayer in vivo, and that helices B and D lie, respectively, along the outer and inner surfaces of the membrane. Molecular organization in the N- and C-terminal regions of the molecule is discussed in terms of evidence from the present work and from other recent investigations.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 25 (1986), S. 959-973 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The changes in optical activity that accompany and characterize the coil-helix and helix-coil transitions of agarose in aqueous solutions and gels have been investigated by combined quantitative analysis of data from vacuum ultraviolet circular dichroism (VUCD) and optical rotary dispersion (ORD). VUCD of agarose in the high-temperature coil state shows a single accessible Gaussian band centered at ∼183 nm. In the helix state this band is blue-shifted by ∼9 nm, and the intensity is increased by a factor of ∼2.6. Spectra at intermediate temperatures can be fitted to within experimental error by linear combination of coil and helix spectra, the relative proportions required providing an index of the extent of conformational ordering. ORD spectra throughout the conformational transition have a common form and differ only in absolute magnitude. The temperature course of conformational ordering derived from ORD intensity is in close agreement with the values obtained from VUCD. In both the coil and helix states the accessible VUCD band is positive, while the overall ORD is negative, indicating strong negative CD activity at lower wavelength. The ORD contribution corresponding to the positive VUCD band was calculated by Kronig-Kramers transform, and it was subtracted from the total ORD to give the residual ORD from all other optically active transitions of the molecule. In both the coil and helix states, this residual ORD could be fitted to within experimental error by a single Gaussian CD band at ∼149 nm. A negative band at this wavelength has been reported previously for agarose films, but the observed intensity, relative to that of the lower energy positive band, is substantially smaller than the fitted value under hydrated conditions. In both the coil and helix states the total optical activity of agarose, characterized by observed ORD spectra, can be matched to within experimental error by Kronig-Kramers transform of the 149-nm negative band and the smaller positive band at higher wavelength, with no necessary involvement of deeper-lying transitions. The significance of this conclusion for fundamental understanding of carbohydrate optical activity is discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The vacuum-uv CD of agarose solid films has been measured to 145 nm and shows a positive band near 180 nm and a larger negative band at around 152 nm. The positive band remains accessible in aqueous solution and has been used to characterize changes in molecular conformation and interaction during the sol-gel transition. The temperature profile of vacuum-uv CD shows sharp, discontinuous changes around the melting and setting points of the gel, which are interpreted in terms of cooperative intermolecular association through double helices, and pronounced hysteresis, which is discussed in terms of helix-helix aggregation.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 25 (1986), S. 1009-1029 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Nongelling solutions of structurally regular chain segments of agarose sulphate show disorder-order and order-disorder transitions (as monitored by the temperature dependence of optical rotation) that are closely similar to the conformational changes that accompany the sol-gel and gel-sol transitions of the unsegmented polymer. The transition midpoint temperature (Tm) for formation of the ordered structure on cooling is ∼25 K lower than Tm for melting. Salt-induced conformational ordering, monitored by polarimetric stopped-flow, occurs on a millisecond time scale, and follows the dynamics expected for the process 2 coil ⇌ helix. The equilibrium constant for helix growth (s) was calculated as a function of temperature from the calorimetric enthalpy change for helix formation (ΔHcal = -3.0 ± 0.3 kJ per mole of disaccharide pairs in the ordered state), measured by differential scanning calorimetry. The temperature dependence of the nucleation rate constant (knuc), calculated from the observed second-order rate constant (kobs) by the relationship kobs = knuc(1 - 1/s) gave the following activation parameters for nucleation of the ordered structure of agarose sulphate (1 mg mL-1; 0.5M Me4NCl or KCl): ΔH* = 112 ± 5 kJ mol-1; ΔS* = 262 ± 20 J mol-1 K-1; ΔG*298 = 34 ± 6 kJ mol-1; (knuc)298 = (7.5 ± 0.5) × 106 dm3 mol-1 s-1. The endpoint of the fast relaxation process corresponds to the metastable optical rotation values observed on cooling from the fully disordered form. Subsequent slow relaxation to the true equilibrium values (i.e., coincident with those observed on heating from the fully ordered state) was monitored by conventional optical rotation measurements over several weeks and follows second-order kinetics, with rate constants of (2.25 ± 0.07) × 10-4 and (3.10 ± 0.10) × 10-4 dm3 mol-1 s-1 at 293.7 and 296.2 K, respectively. This relaxation is attributed to the sequential aggregation processes helix + helix → dimer, helix + dimer → trimer, etc., with depletion of isolated helix driving the much faster coil-helix equilibrium to completion. Light-scattering measurements above and below the temperature range of the conformational transitions indicate an average aggregate size of 2-3 helices.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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