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Angaben zur Quelle [Bearbeiten]

Autor     Chartchalerm Isarankura-Na-Ayudhya & Tanawut Tantimongcolwat & Hans-Joachim Galla & Virapong Prachayasittikul
Titel    Fluorescent Protein-Based Optical Biosensor for Copper Ion Quantitation
Zeitschrift    Biol Trace Elem Res
Jahr    2010
Seiten    352–363
Anmerkung    online 2009
URL    http://www.pubfacts.com/detail/19649570/Fluorescent-protein-based-optical-biosensor-for-copper-ion-quantitation.

Literaturverz.   

yes
Fußnoten    yes
Fragmente    4


Fragmente der Quelle:
[1.] Tim/Fragment 017 15 - Diskussion
Zuletzt bearbeitet: 2014-10-27 04:37:00 Hindemith
Fragment, Gesichtet, Isarankura 2009, SMWFragment, Schutzlevel sysop, Tim, Verschleierung

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Seite: 17, Zeilen: 15-16
Quelle: Isarankura 2009
Seite(n): 353, Zeilen: 17 ff.
Recently, the fluorescent proteins from various organisms become potential candidates for sensor development. These [include the green fluorescent protein and its variants, the red fluorescent protein (DsRed) from the tropical coral namely Discosoma sp.] Recently, the fluorescent proteins from various organisms become potential candidates for sensor development. These include the green fluorescent protein (GFP) and its variants from the Pacific Northwest jellyfish namely Aequorea victoria [7–11], the red fluorescent protein (DsRed) from the tropical coral namely Discosoma sp. [12–14], and the far-red fluorescent (HcRed) protein from the reef coral namely Heteractis crispa [15, 16].
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The source is not given here, but will be mentioned on page 19.

The text of the source has been shortened in a way that is little consistent with normal English language usage.

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(SleepyHollow02), Hindemith

[2.] Tim/Fragment 018 01 - Diskussion
Zuletzt bearbeitet: 2014-10-27 05:00:24 Hindemith
Fragment, Gesichtet, Isarankura 2009, KeineWertung, SMWFragment, Schutzlevel sysop, Tim

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Quelle: Isarankura 2009
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[These] include the green fluorescent protein and its variants, the red fluorescent protein (DsRed) from the tropical coral namely Discosoma sp.

Richmond et al. (2000) have introduced metal-binding sites onto the surface of GFP and found that these metal-binding mutants of GFP exhibited fluorescence quenching at lower transition metal ion (Cu2+, Ni2+, or Co2+) concentrations (104) than those of the wild-type protein.

These include the green fluorescent protein (GFP) and its variants from the Pacific Northwest jellyfish namely Aequorea victoria [7–11], the red fluorescent protein (DsRed) from the tropical coral namely Discosoma sp. [12–14], and the far-red fluorescent (HcRed) protein from the reef coral namely Heteractis crispa [15, 16].

[...] By the same year, Richmond and his colleagues have introduced metal-binding sites onto the surface of GFP and found that metals in close proximity to chromophores are known to quench fluorescence in a distance-dependent fashion [8].

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The copied text starts on the previous page: Tim/Fragment 017 15‎

The source is not mentioned here. It will be mentioned on page 19.

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(SleepyHollow02), Hindemith

[3.] Tim/Fragment 019 03 - Diskussion
Zuletzt bearbeitet: 2014-11-27 22:12:51 Hindemith
BauernOpfer, Fragment, Gesichtet, Isarankura 2009, SMWFragment, Schutzlevel sysop, Tim

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Quelle: Isarankura 2009
Seite(n): 352, Zeilen: abstract
Isarankura et al. (2009) explored spectroscopic determinations of copper ions using chimeric metal-binding green fluorescent protein His6GFP (espressed in E. coli and purified to homogeneity) as an active indicator. Supplementation of copper ions to the GFP solution led to a remarkable decrease of fluorescent intensity corresponding to metal concentrations. For circumstances, rapid declining of fluorescence up to 60% was detected in the presence of 500 μM copper. This was in contrast to those observed in the case of zinc and calcium ions, in which approximately 10–20% of fluorescence was affected (fig. 11). Recovery of its original fluorescence up to 80% was mediated by the addition of EDTA.

More importantly, in the presence of metal ions, the emission wavelength maximum remained unchanged while reduction of the optical density of the absorption spectrum has been observed. This indicated that the chromophore‟s ground state was possibly affected by the static quenching process rather than structural or conformational alteration.

Abstract

In the present study, spectroscopic determinations of copper ions using chimeric metal-binding green fluorescent protein (His6GFP) as an active indicator have been explored. Supplementation of copper ions to the GFP solution led to a remarkable decrease of fluorescent intensity corresponding to metal concentrations. For circumstances, rapid declining of fluorescence up to 60% was detected in the presence of 500 μM copper. This is in contrast to those observed in the case of zinc and calcium ions, in which approximately 10–20% of fluorescence was affected. Recovery of its original fluorescence up to 80% was mediated by the addition of ethylenediamine tetraacetic acid. More importantly, in the presence of metal ions, the emission wavelength maximum remains unchanged while reduction of the optical density of the absorption spectrum has been observed. This indicates that the chromophore’s ground state was possibly affected by the static quenching process.

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The source is given, but it is not clear to the reader that the following text is taken from it. The copied text includes, what could be understood as an interpretation / evaluation of the results of the source: "a remarkable decrease", "More importantly", "This indicated that", "possibly".

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(SleepyHollow02), Hindemith

[4.] Tim/Fragment 023 03 - Diskussion
Zuletzt bearbeitet: 2014-10-27 04:52:36 Hindemith
Fragment, Gesichtet, Isarankura 2009, SMWFragment, Schutzlevel sysop, Tim, Verschleierung

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Seite: 23, Zeilen: 3-5
Quelle: Isarankura 2009
Seite(n): 353, Zeilen: last lines
Engineered E. coli co-expressing surface exposed zinc-binding motif and GFP has been applied for real-time monitoring of intracellular mobility of zinc ions (Isarankura-Na-Ayudhya et al., 2005).

Isarankura-Na-Ayudhya C., Suwanwong Y., Boonpangrak S., Kiatfuengfoo R., Prachayasittikul V., 2005. Co-expression of zinc binding motif and GFP as a cellular indicator of metal ions mobility. Int. J. Biol. Sci., 1: 146-151.

Additionally, engineered E. coli co-expressing surface exposed zinc-binding motif and GFP has been applied for real-time monitoring of intracellular mobility of zinc ions [27].

27. Isarankura-Na-Ayudhya C, Suwanwong Y, Boonpangrak S et al (2005) Co-expression of zinc binding motif and GFP as a cellular indicator of metal ions mobility. Int J Biol Sci 1:146–151

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(SleepyHollow02), Hindemith

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