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  • Protein kinase C  (4)
  • Chemistry  (3)
  • Light induction  (3)
  • Amylase release  (2)
  • 1
    ISSN: 0014-5793
    Keywords: Gene expression ; Gene-dosage regulation ; Light induction ; Ribulosebisphosphate carboxylase ; Transcriptional regulation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 239 (1988), S. 199-202 
    ISSN: 0014-5793
    Keywords: (Pea seedling) ; Action spectrum ; Green light ; Light induction ; Photogene expression ; Phytochrome ; Violet light
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 276 (1990), S. 161-164 
    ISSN: 0014-5793
    Keywords: Down-regulation ; Myosin light chain ; Protein kinase C ; Smooth muscle cell line ; Staurosporine
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0014-5793
    Keywords: Carbon tetrachloride administration ; DNA synthesis ; Liver regeneration ; Protein kinase C
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 196 (1986), S. 171-174 
    ISSN: 0014-5793
    Keywords: (Pea seedling) ; Gene dosage ; Light induction ; Phytochrome Ribulose-bisphosphate carboxylase ; chloroplast DNA
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 320 (1993), S. 47-51 
    ISSN: 0014-5793
    Keywords: Lysophosphatidylcholine ; Phospholipase A"2 ; Protein kinase C
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-2013
    Keywords: Key words Smooth muscle cell ; Myosin light chain mono and diphosphorylation ; Phosphatase ; Protein kinase C
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The characteristics of actively growing smooth muscle cells (a variant, SM-3) were compared with those of growth-arrested cells with regard to response of myosin light chain (MLC) phosphorylation. Augmented MLC phosphorylation, in particular diphosphorylation, was observed in actively growing cells when stimulated with 30 μM prostaglandin F2α (PGF2α). The maximum level of diphosphorylation in growing cells was significantly higher than that in growth-arrested cells. The MLC diphosphorylation was sensitive to protein kinase C down-regulation by phorbol dibutylate and pretreatment by the protein kinase inhibitors, staurosporine (30 nM) and isoquinoline sulphonamide HA1077 (20 μM). The actively growing cells contained larger amounts of protein kinase C than growth-arrested cells. The phosphorylation sites of mono- and diphospho-MLC were determined to be MLC kinase-dependent sites (Thr18, Ser19). The PGF2αconcentration/response curves of MLC diphosphorylation were shifted to the left and upwards in the presence of the protein phosphatase inhibitor calyculin A. These results suggest that PGF2αstimulation of actively growing SM-3 cells augments MLC kinase-dependent MLC diphosphorylation. Protein kinase C is involved indirectly in this reaction, possibly through MLC phosphatase-sensitive regulatory mechanisms.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 166 (1996), S. 305-309 
    ISSN: 1432-136X
    Keywords: Key words Exocrine pancreas ; Fatty acids ; Amylase release ; Sheep ; Rats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Stimulatory effects of saturated fatty acids consisting of 4 (butyrate), 8 (octanoate), 12 (laurate) and 16 (palmitate) carbon atoms, as well as acetylcholine on pancreatic amylase release were assessed in tissue segments isolated from sheep, rats, hamsters, field voles and mice. The amount of amylase release induced by the fatty acids (1 μmol ⋅ l-1 to 10 mml ⋅ l-1) and by acetylcholine (10 nmol ⋅ l-1 to 100 μmol ⋅ l-1) increased in a concentration-dependent manner, and the maximum response in response to the fatty acids was obtained at the maximal dose used. The maximum increase in amylase release in response to butyrate or octanoate was highly and significantly (r=0.974, P〈0.001) dependent on the log value of the mean body mass in the following order: sheep〉rats〉hamsters〉field voles〉mice. On the other hand, the response to laurate and palmitate was variable among animal species. Addition of atropine (1.4 μmol ⋅ l-1) to the medium did not reduce the responses to octanoate stimulation, but significantly reduced acetylcholineinduced responses, implying that the effects of the fatty acids were not mediated through activation of muscarinic acetylcholine receptors. Reduction of calcium ion concentration in the medium significantly inhibited the responses induced by the fatty acids and acetylcholine, suggesting that amylase release depends on extracellular calcium ions.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 166 (1996), S. 305-309 
    ISSN: 1432-136X
    Keywords: Exocrine pancreas ; Fatty acids ; Amylase release ; Sheep ; Rats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Stimulatory effects of saturated fatty acids consisting of 4 (butyrate), 8 (octanoate), 12 (laurate) and 16 (palmitate) carbon atoms, as well as acetylcholine on pancreatic amylase release were assessed in tissue segments isolated from sheep, rats, hamsters, field voles and mice. The amount of amylase release induced by the fatty acids (1 μmol·l−1 to 10 mml·l−1) and by acetylcholine (10 nmol·l−1 to 100 μmol·l−1) increased in a concentration-dependent manner, and the maximum response in response to the fatty acids was obtained at the maximal dose used. The maximum increase in amylase release in response to butyrate or octanoate was highly and significantly (r=0.974,P〈0.001) dependent on the log value of the mean body mass in the following order: sheep 〉 rats 〉 hamsters 〉 field voles 〉 mice. On the other hand, the response to laurate and palmitate was variable among animal species. Addition of atropine (1.4 μmol·l−1) to the medium did not reduce the responses to octanoate stimulation, but significantly reduced acetylcholine-induced responses implying that the effects of the fatty acids were not mediated through activation of muscarinic acetylcholine receptors. Reduction of calcium ion concentration in the medium significantly inhibited the responses induced by the fatty acids and acetylcholine, suggesting that amylase release depends on extracellular calcium ions.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 487 (1982), S. 232-240 
    ISSN: 0044-2313
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: High Temperature Phosphidation of Iron-Nickel Alloys by Phosphorus VaporA study was undertaken concerning the products and kinetics in the phosphidation of iron-nickel alloys with various ratios of metallic constituents at 700° in phosphorus vapor at 1 atm by a sealed-tube method. X-ray diffraction patterns and an electron microprobe analysis of the products showed that the phosphide-layer structure reaches the expression of NiP2 ∼ Ni6P5/Ni2P, Fe2P/(Fe—Ni alloy). The phosphidations proceeded according to a parabolic rate law for all the compositions of the alloy. A marker experiment indicated that the diffusing species was not phosphorus but metals. The rate constant decreased with an increase in the content of iron in the alloy.
    Notes: Reaktionsprodukte und Kinetik bei der Phosphidierung von Eisen-Nickellegierungen verschiedener Zusammensetzung bei 700° in Phosphordampf (1 atm) im geschlossenen Quarzrohr wurden untersucht. Aus Röntgenbeugungsbildern und Elektronenstrahlmikrosondeanalysen der Produkte folgt, daß sich Phosphidschichten von NiP2 ∼ Ni6P5/Ni2P, Fe2P/(Fe—Ni-Legierung) bilden. Die Phosphidierungen an Legierungen aller Zusammensetzungen verliefen nach dem parabolischen Zeitgesetz. Ein Markierungsversuch zeigte, daß nicht der Phosphor, sondern die Metalle diffundieren. Die Geschwindigkeitskonstante nahm mit zunehmendem Eisengehalt der Legierung ab.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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