Determination of Cerium (IV) Using Rhodamine 6G Fluorescence Quenching

In the condition of 1.24 mmol/L EDTANa2, 16.7 mmol/L NaCl and 0.17 mmol/L Tris, the substrate chain of double-stranded DNA (dsDNA) could be cracked by Pb2+ to release single-stranded DNA (ssDNA) that adsorb onto AuPd nanoparticle (AuPdNP) and form stable AuPdNP-ssDNA, but the dsDNA can not protect AuPdNP that were aggregated to big AuPdNP aggregations (AuPdNPA) under the action of NaCl. The AuPdNP-ssDNA and AuPdNPA could be separated by centrifugation. With the concentration of Pb2+ increased, the released ssDNA increased, the AuPdNP-ssDNA in centrifugation solution increased and the catalytic effect enhanced on the fluorescence quenching reaction of Rhodamine 6G (Rh6G) and NaH2PO2, which led the fluorescence intensity at 552nm to decrease. The decreased fluorescence intensity (ΔF552nm) was linear to the concentration of Pb2+ in the range of 0.33-8.00 nmol/L, a detection limit of 0.21 nmol/L. The proposed method was applied to detect Pb2+ in water samples, with satisfactory results.

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Determination of chromium in waste-water and cast iron samples by fluorescence quenching of rhodamine 6G

Talanta ◽

10.1016/s0039-9140(97)00261-0 ◽

1998 ◽

Vol 46 (1) ◽

pp. 215-219 ◽

Cited By ~ 24

Author(s):

N Jie

Keyword(s):

Waste Water ◽

Cast Iron ◽

Fluorescence Quenching ◽

Rhodamine 6G

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Fluorescence quenching determination of iron(iii) using rhodamine 6G hydrazide derivative

Analytical Methods ◽

10.1039/c3ay26492k ◽

2013 ◽

Vol 5 (7) ◽

pp. 1843 ◽

Cited By ~ 10

Author(s):

Chunhua Ma ◽

Liping Lin ◽

Yanyan Du ◽

Liang-bi Chen ◽

Feng Luo ◽

...

Keyword(s):

Fluorescence Quenching ◽

Rhodamine 6G ◽

Hydrazide Derivative

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A Homogeneous Nonisotopic Histone Deacetylase Activity Assay

CrossRef Listing of Deleted DOIs ◽

10.1177/1087057102239644 ◽

2003 ◽

Vol 8 (1) ◽

pp. 89-95 ◽

Cited By ~ 21

Author(s):

Birgit Heltweg ◽

Manfred Jung

Keyword(s):

Drug Discovery ◽

Fluorescence Quenching ◽

Histone Deacetylase ◽

Anticancer Agents ◽

Histone Deacetylases ◽

Activity Assay ◽

Animal Testing ◽

Hdac Activity

Histone deacetylases (HDACs) are important regulators of transcription, and their inhibitors are a promising class of anticancer agents. The methods for the determination of HDAC activity and its inhibition that are currently available suffer from various drawbacks, such as animal testing, radioactive substrates, or limited throughput. Therefore, a fast nonisotopic method for the measurement of HDAC activity is highly desirable. The authors present such an assay that relies on the fluorescent HDAC substrate developed previously in their group. After incubation of the substrate with the enzyme, a derivatization leads to efficient fluorescence quenching in the deacetylated metabolite. Thus, only the fluorescence emitted by the remaining substrate is detected, which allows for a convenient detection of HDAC activity in a homogeneous format that can be performed on multiwell plate readers. This procedure, called HDASH (histone deacetylase assay—homogeneous), should be a valuable tool in transcriptional research and especially drug discovery. ( Journal of Biomolecular Screening 2003:89-95)

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