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  • 1990-1994  (5)
  • 1993  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 62 (1993), S. 2504-2506 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A Co-22 at. % magnetic thin film, sputter deposited on a heated Cu coated Si substrate, was analyzed in the planar direction of the film by atom probe field ion microscopy (APFIM). The atom probe concentration depth profile convincingly showed that the film contained two phases, one enriched in Cr up to 30–35 at. % and the other enriched in Co up to 95–93 at. %. This result indicates that Co-22 at. % Cr thin film deposited on a heated substrate consists of ferromagnetic and paramagnetic phases, each less than a few tens of nanometers in size.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Fatigue & fracture of engineering materials & structures 16 (1993), S. 0 
    ISSN: 1460-2695
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract— The basic fatigue strength of welded joints in four steels having different yield strengths has been obtained by tests in which the maximum applied stress was held constant and equal to the yield strength, to simulate the tensile residual stress in real large-scale structures. In the long-life region superior properties occurred with a decrease in the yield strength. It is therefore suggested that both low yield strength steel, which can be produced by a thermo-mechanical control process without affecting the tensile strength, and steels or welding consumables which show a low transformation temperature, may have a high fatigue strength.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0428
    Keywords: Glucose transporter ; embryogenesis ; hyperglycaemia ; rat embryo culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We investigated the expression of glucose transporter genes and protein in embryo and yolk sac during organogenesis and the regulation of glucose transporters during culture in hyperglycaemic media. Erythrocyte-type glucose transporter (GLUT 1) and brain-type glucose transporter (GLUT 3) mRNA were expressed in embryo and yolk sac. The expression of GLUT-1 and GLUT-3 mRNA was abundant on day 9–11 and day 9–10 in the embryo, respectively, and day 9–14 and day 10–11 in the yolk sac, respectively. The levels of GLUT-1 protein in the embryo increased in parallel with the expression of GLUT-1 mRNA during the corresponding period. Immunohistochemical staining of GLUT-1 protein was found principally in the neuroepithelial cells surrounding the neural tube in the embryo on day 10 and appeared in the microvessels surrounding the neural tube after day 12. To test whether the expression of glucose transporter genes and protein was suppressed during hyperglycaemia, conceptuses were cultured in high glucose medium. The abundant expression of GLUT-1 protein was not decreased during culture in high glucose media for 24 h (day 9–10) and was only down-regulated by prolonged exposure to this media for 48 h (day 9–11). We have demonstrated the predominant expression of the high affinity glucose transporter (GLUT 1 and GLUT 3) genes and (GLUT 1) protein in embryo during the early period of organogenesis. The persistently abundant expression of glucose transporter during the critical period of neural tube formation (day 9–10) even in the presence of hyperglycaemia may explain one of the mechanisms of increased glucose flux into the neuroepithelium, which may lead to neural tube defects.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-5233
    Keywords: Embryogenesis ; Glucose transporter ; Growth retardation ; Hypoglycemia ; Neural tube defect ; Rat embryo culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We investigated the glucose transporter gene and protein expression during early organogenesis in the rat and in rat embryos cultured with hypoglycemic serum. Erythrocyte-type glucose transporter (GLUT-1) mRNA was expressed at a high level in embryos; peak levels were reached at days 10.5–11.5 and decreased as gestational age increased. In contrast, the insulin regulaable glucose transporter (GLUT-4) mRNA was not detected. The levels of GLUT-1 protein determined by Western blot analysis increased in parallel with expression of the glucose transporter (GLUT-1) gene and peak levels were observed on days 10.5 and 11.5, which correspond to the main periods of neural tube formation. Immunohistochemical staining of the embryo on day 10.5 showed that GLUT-1 protein was abundantly located in the tissue of neural tube. When embryos were cultured from day 9.5 to day 10.5 with insulin-induced hypoglycemic serum containing 2–3 mM glucose an increased frequency of anterior neural tube defects was observed in association with a significant reduction of the glycolytic flux. Increased levels of GLUT-1 mRNA and protein were not observed during the culture with hypoglycemic serum compared with the levels in embryos cultured in normal serum. Addition of insulin to normal serum (500 μU/ml) did not affect the GLUT-1 mRNA and protein levels. GLUT-1 mRNA and protein are strongly expressed in the embryo during early organogenesis, especially in the tissues of the neural tube, and the expression of the glucose transporter did not increase in response to prolonged glycopenia. This may account for the vulnerability of embryogenesis to hypoglycemia during these critical developmental periods.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Hyperfine interactions 80 (1993), S. 1099-1102 
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract New spin-crossover complexes [Fe(III)L(lut)]BPh4 (L = mbpN or bpN) with N4O2 moiety are reported. The structure of the mbpN (N3O2 quinquedentate ligand) complex is determined at 293 K, and the temperature dependences of the57Fe Mössbauer spectra and magnetic susceptibilities for both complexes have been examined.
    Type of Medium: Electronic Resource
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