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  • 1
    Electronic Resource
    Electronic Resource
    Limited acclimation of photosynthesis to blue light in the seaweed Gracilaria tenuistipitata (2002)
    Oxford, UK : Munksgaard International Publishers
    Physiologia plantarum 114 (2002), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Changes in photosynthetic capacity of the seaweed Gracilaria tenuistipitata Zhang et Xia acclimated to monochromatic blue light were studied. For this purpose, affinity for external inorganic carbon, light use efficiency, carbonic anhydrase (CA; EC 4.2.1.1) activity and content of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) were determined in thalli acclimated to 45 µmol m−2 s−1 of blue light. Thalli cultured in white light of the same photon fluence rate were used as a control. Lower maximal photosynthetic rates (i.e. at light and carbon saturation) were obtained in the thalli cultured in blue light. Apparently, this lower photosynthetic capacity was not due to differences in affinity and/or capacity for use of external dissolved inorganic carbon (DIC) since (1) CA activity did not change significantly and (2) similar values of photosynthetic conductance for DIC at alkaline pH were obtained (0.95 × 10−6 m s−1). In addition, the pool size of Rubisco was not modified by the blue light treatment since there were no significant differences in Rubisco content between white (12.14% of soluble proteins) and blue light (12.13% of soluble proteins) treatments. In contrast, Fv/Fm was increased by 11% and photosynthetic efficiency for oxygen production was reduced by 50% in blue light. This absence of correlation between quantum yields for maximum stable charge separation of photosystem II and oxygen evolution suggests that blue light promote changes in rates of photosynthetic electron flow.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2002.1140319.x
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  • 2
    Electronic Resource
    Electronic Resource
    Peroxidase-ferrocene modified carbon paste electrode as an amperometric sensor for the hydrogen peroxide assay (1991)
    Weinheim : Wiley-Blackwell
    Electroanalysis 3 (1991), S. 281-285 
    Details
    ISSN: 1040-0397
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A new enzymatic amperometric sensor for hydrogen peroxide based on a modified carbon paste electrode is described. Horseradish peroxidase and ferrocene mediator were immobilized by dissolution or dispersion in a graphite-paraffin oil paste. To prevent losses of immobilized chemicals under operational conditions, the electrode surface was coated with a Nafion membrane. The device exhibits a relatively fast response time (42 s for 95% of the steady-state response) and yields currents linearly related to the hydrogen peroxide concentration over the 10-7 to 10-5 mol/L range in both static and flow injection operations. The slope of the calibration plot remained constant for more than 20 days. Flow injection assays of hydrogen peroxide at a sampling rate of about 70 injections per hour, with a relative standard deviation of 1.4%, are possible. An easy and low cost preparation procedure is described.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elan.1140030407
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Flow-injection analysis of hydrogen peroxide using a horseradish peroxidase-modified electrode detection system (1990)
    Weinheim : Wiley-Blackwell
    Electroanalysis 2 (1990), S. 303-308 
    Details
    ISSN: 1040-0397
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A flow-injection analysis (FIA) system utilizing a horseradish peroxidase-modified amperometric electrode is described. The enzyme was immobilized through adsorption onto a glassy carbon electrode, and the system is used to determine hydrogen peroxide at submicromolar levels. The response is based on the enzymatic reduction of hydrogen peroxide in the presence of hydroquinone acting as an electron mediator. The oxidized quinone produced in the enzymatic reaction is reduced at the electrode, and the reduction current was found to be proportional to the concentration of hydrogen peroxide. Calibration curves were found to be linear between 2.5 × 10-8 and 1.0 × 10-6 M, and the method has a detection limit of 1.0 × 10-8 M.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elan.1140020407
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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