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  • 1
    ISSN: 1572-8838
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Electrical Engineering, Measurement and Control Technology
    Notes: Abstract Electrolysis at the interface between a Na(AuCl4)–CuSO4 aqueous phase and an immiscible hexyl acetate phase resulted in continuous growth of gold films along the interface. To maintain filmy growth of gold, it was effective to stimulate displacement of predeposited copper with gold by applying a rectangular or triangular potential in a given range. Two types of electrodes were applied: from a point electrode the film grew concentrically like a blooming flower, and from a line electrode the film grew unidirectionally toward the counter electrode as a spreading wave. A long time electrolysis could be performed by circulating and filtering the aqueous solution. The film contained no trace of copper and was very thin (〈1μm).
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1440
    Keywords: Key words Human T-lymphotropic virus type I ; Hashimoto’s thyroiditis ; Envelope protein ; Messenger RNA ; In situ hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Human T-lymphotropic virus type I (HTLV-I) protein and messenger RNA (mRNA) for HTLV-I were examined in thyroid tissues from two patients with Hashimoto’s thyroiditis and serum anti-thyroid antibody. The virus envelope protein and signals for the mRNA were detected in many of the follicular epithelial cells of the thyroid tissue from one of the patients, respectively, by immunohistochemistry and in situ hybridization. PCR–Southern blotting revealed the presence of HTLV-I DNA in the thyroid tissue, in which the viral protein and mRNA were detected, although no virus particles were found in the epithelial cells by electron microscopy. HTLV-I virus was not present in the thyroid tissue from the second patient. The present findings suggest that infection of thyroid tissue with HTLV-I is associated with the pathogenesis of Hashimoto’s thyroiditis in some patients.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1440
    Keywords: Human T-lymphotropic virus type I ; Hashimoto's thyroiditis ; Envelope protein ; Messenger ; RNA ; In situ hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Human T-lymphotropic virus type I (HTLV-I) protein and messenger RNA (mRNA) for HTLV-I were examined in thyroid tissues from two patients with Hashimoto's thyroiditis and serum anti-thyroid antibody. The virus envelope protein and signals for the mRNA were detected in many of the follicular epithelial cells of the thyroid tissue from one of the patients, respectively, by immunohistochemistry and in situ hybridization. PCR-Southern blotting revealed the presence of HTLV-I DNA in the thyroid tissue, in which the viral protein and mRNA were detected, although no virus particles were found in the epithelial cells by electron microscopy. HTLV-I virus was not present in the thyroid tissue from the second patient. The present findings suggest that infection of thyroid tissue with HTLV-I is associated with the pathogenesis of Hashimoto's thyroiditis in some patients.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Development genes and evolution 204 (1995), S. 418 
    ISSN: 1432-041X
    Keywords: Lepidopteran insect ; Butterfly wing ; Programmed cell death ; Apoptosis ; Wing morphogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The outline of the adult wing of lepidopteran insects (butterflies and moths) emerges as a result of disappearance of a group of cells at the periphery of the pupal wing. Histological observation of the pupal wing of Pieris rapae showed that, just after apolysis of the wing epithelium from the pupal cuticle, there occurs a rapid and localized decrease of the number of cells at the periphery of the wing. This decrease occurs through cell death, which lasts 1–1.5 days at 20°C. Dying cells lose contact with the neighbouring cells and show condensation of chromatin and cytoplasm. They then appear to be phagocytosed by neighbouring epithelial cells or discharged through the basal surface of the epithelium into the lumen within the wing and taken up by phagocytes. Fragmentation of DNA in the nuclei was detected in the dead cells or their debris. These results indicate that programmed cell death in the lepidopteran wing proceeds through a mechanism closely similar to that of apoptosis in the vertebrate.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-2048
    Keywords: Key words: Abscisic acid (analog) ; α-Amylase I-1 ; Gene expression (RAmy1A) ; Oryza (α-amylase ; sugar accumulation) ; Sugar accumulation (rice)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The effects of (+)-8′,8′,8′-trifluoroabscisic acid (trifluoro-ABA) on α-amylase expression were studied in rice embryoless half-seeds, scutella, and suspension-cultured cells derived from the embryo, and the effects of the analog on sugar accumulation were also studied in scutella and suspension-cultured cells. Treatment with (+)-trifluoro-ABA strongly inhibited the gibberellic acid-inducible expression of α-amylase I-1 encoded by RAmy1A in the aleurone layers of embryoless half-seeds at the levels of transcription, protein synthesis, and enzyme activity. It was also found that (+)-trifluoro-ABA stimulated (i) the uptake of glucose from the incubation medium and (ii) the synthesis of sucrose in scutellar tissues and suspension-cultured cells of rice. The biological activity of (+)-trifluoro-ABA was found to be more potent and persistent than that of natural ABA. We further examined the effects of trifluoro-ABA on the expression of α-amylase I-1 in scutellar tissues and suspension-cultured cells. It was found that (+)-trifluoro-ABA did not inhibit the formation of α-amylase I-1 in the absence of external glucose. However, glucose and (+)-trifluoro-ABA cooperatively suppressed the formation of α-amylase I-1. Judging from these results, we conclude that the regulatory mechanism for the expression of α-amylase I-1 in the scutellar epithelium is distinguishable from that operating in the aleurone layer.
    Type of Medium: Electronic Resource
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