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  • Analytical Chemistry and Spectroscopy  (2)
  • Cell & Developmental Biology  (2)
  • NH 4 + assimilation  (1)
  • 1980-1984  (5)
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Keywords
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 159 (1983), S. 483-486 
    ISSN: 1432-2048
    Keywords: Ammonium assimilation ; Glutamate dehydrogenase ; Hordeum ; NH 4 + assimilation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Enzyme assays of the roots of barley (Hordeum vulgare L.) fed NH 4 + show high glutamate-dehydrogenase (GDH; EC 1.4.1.3) activity compared with glutamine-synthetase (GS; EC 6.3.1.2) activity, indicating that GDH may be involved in ammonium assimilation in the root. When 15NH 4 + is fed to barley roots, a high accumulation of 15N takes place in free amino compounds, particularly glutamine and glutamate. When the GS inhibitor, methionine sulfoximine (MSO), is added to the 15NH 4 + feeding medium the free amino compounds remain unlabelled while 15NH 4 + accumulates rapidly in the roots. Root enzyme assays demonstrate that GS is completely inhibited by MSO treatment, while the activity of GDH remains unaffected. The feeding of 15N-amido glutamine to the roots in the presence of MSO and the subsequent 15N enrichment of the free amino compounds of the root show that MSO does not interfere substantially with nitrogen assimilation after the formation of glutamine. These results indicate that in the barley root, ammonium absorbed from the soil is assimilated entirely via the GS-glutamate synthase (GOGAT) pathway, and that GDH plays little, if any, part in this process.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 104 (1980), S. 73-81 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Resting cultures of primary chick embryo cells have been labeled with 3H-leucine for the first 2 or 3 hours after feeding basal medium or basal medium supplemented with 10% dialyzed serum. The labeling patterns of the 3H-polypeptides of the soluble cell fraction have been compared by fluorography of two-dimensional gels. Large and consistent differences are seen in only three of the more than 900 spots that can visualized. This report concerns two of the three spots. The 3H contents of the two polypeptides (41,000 daltons, pI 7.1, designated 41-7.1, and 34,000 daltons, pI 6.2, designated 34-6.2) are increased by serum by about ten-fold. The highly selective effect of serum on the labeling of the two spots does not appear to be an artifact related to the extractability, solubility, or state of aggregation of the polypeptides. The radio-intensities of both polypeptides decrease markedly when the cells are labeled later than 3 hours after “shift-up”.Drugs that inhibit RNA synthesis and are known to stop the progression of the chick cells through the G1 period, camptothecin, cordycepin and 5,6-dichloro-β-D-ribofuranosylbenzimidazole, depress, with great specificity, the enhanced labeling of polypeptide 41-7.1 in the stimulated cells, and all but camptothecin have a similar action on polypeptide 34-6.2. A high level of actinomycin D (10 μg/ml), but neither a low level of the drug (0.02 μg/ml) nor 5-fluorouridine prevents the increased labeling of the two polypeptides in serum-fed cells. That 5-fluorouridine enters the chick cells and is converted to its active form is shown by the inhibition of the processing of pre-ribosomal RNA.The observations with the RNA inhibitors are at least consistent with the conclusions that the enhanced labeling of the two sports results from increased rates of synthesis of the polypeptïdes that depend upon mRNA production but not on the formation of ribosomal RNAs, and that the polypeptides play a role in the regulation of DNA replication in the chick cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 104 (1980), S. 61-72 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Events that are essential for progression through the G1 period begin immediately or shortly after resting chick embryo cells are given fresh medium with serum. The following observations support the contention that the critical events include the production of non-ribosomal RNAs: (1) Addition to the “shift-up” medium of either of two inhibitors of RNA formation, comptothecin or 5, 6-dichloro-1-β-D-ribofuranosylbenzimidazole, delays the onset of DNA replication by about the length of time the cells are exposed to the drugs. (2) Although entry into the S phase is delayed by the inhibitors, the slopes of the DNA response curves are identical to that of control cultures. (3) Neither drug reduces significantly the rate of overall protein synthesis. Observations (2) and (3) are taken to mean that expansion of the G1 period is not due to cell damage. (4) A third inhibitor of RNA synthesis, cordycepin, also delays passage of stimulated cells throgh the G1 phase, but, in this case, the length of the delay period is greater than that of the exposure period. (5) A low dose of actinomycin D does not impede movement towards the S phase, even though the synthesis of preribosomal RNA is considerably reduced.The possibility is considered that the essential G1 molecules are mRNAs.
    Additional Material: 7 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Journal of Raman Spectroscopy 9 (1980), S. 1-4 
    ISSN: 0377-0486
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The interaction of iodine cyanide and cyanide in aqueous solution has been reinvestigated and it has been confirmed that a complex cyanide ion, the dicyanoiodate(I) ion [I(CN)2]- is formed. This ion has been isolated in the solid state for the first time, as its tetraphenylarsonium, tetraphenylphosphonium and caesium salts. Infrared and Raman spectroscopic studies of these salts are reported. These spectra are fully consistent with a linear centrosymmetric (D∞h) structure for the [I(CN)2]-ion. Assignments are made for six of the seven fundamentals of the [I(CN)2]-ion in the caesium salt.
    Additional Material: 6 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Journal of Raman Spectroscopy 9 (1980), S. 209-213 
    ISSN: 0377-0486
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The [I2CN]- ion, previously only known in aqueous solution, has been isolated as its caesium salt; and the previously unknown [BrICN]- ions [ClICN]- have been isolated as their caesium salts. The Raman and IR vibrational spectra of these three caesium salts have been investigated in detail and indicate that the halide ions coordinate to the I atom of ICN to form linear (C∞ν) [X - I - CN]- ions (X=I, Br or Cl), contained in a centrosymmetric unit cell. This C∞ν structure is supported by a normal coordinate analysis for the [IICN]- ion.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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