scholarly journals Determination of 3-Methyl-quinoxaline-2-carboxylic Acid and Quinoxaline-2-carboxylic Acid in Pork Based on a Background Fluorescence Quenching Immunochromatographic Assay

2020 ◽  
Vol 36 (7) ◽  
pp. 783-785
Author(s):  
Xulin WAN ◽  
Xin WANG ◽  
Xiaoqi TAO
2017 ◽  
Vol 2017 ◽  
pp. 1-7 ◽  
Author(s):  
Xiaoxia Wu ◽  
Xiaofeng Tian ◽  
Lihua Xu ◽  
Jiutong Li ◽  
Xinxia Li ◽  
...  

Harsh demanding has been exposed on the concentration of aflatoxin M1 (AFM1) and chloramphenicol (CAP) in milk. In this study, we developed a new method based on background fluorescence quenching immunochromatographic assay (bFQICA) to detect AFM1 and CAP in milk. The detection limit for AFM1 was 0.0009 ng/mL, while that for the CAP was 0.0008 ng/mL. The assay variability was determined with 3 AFM1 standards (i.e., 0.25 ng/mL, 0.5 ng/mL, and 1.0 ng/mL), and the actual detection value was 0.2497, 0.5329, and 1.0941, respectively. For the assay variability of 3 CAP standards (i.e., 0.10 ng/mL, 0.30 ng/mL, and 0.50 ng/mL), the actual detection value was 0.0996, 0.3096, and 0.4905, respectively. The recovery rate of AFM1 was 99.7%–101.7%, while that for CAP was 95.3%–97.6%. For the test stability, AFM1 and CAP showed satisfactory test stability even at month 5. Compared with the sensitivity of liquid chromatography-mass spectrometry (LC-MS) method, no statistical difference was noticed in results of the bFQICA. Our method is convenient for the detection of AFM1 and CAP in milk with a test duration of about 8 minutes. Additionally, an internal WiFi facility is provided in the system allowing for quick connection and storage in the intelligent cell phone.


2014 ◽  
Vol 841 ◽  
pp. 44-50 ◽  
Author(s):  
Xiangjun Chen ◽  
Yangyang Xu ◽  
Jinsheng Yu ◽  
Jiutong Li ◽  
Xuelei Zhou ◽  
...  

2003 ◽  
Vol 8 (1) ◽  
pp. 89-95 ◽  
Author(s):  
Birgit Heltweg ◽  
Manfred Jung

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)


2014 ◽  
Vol 47 (16) ◽  
pp. 2740-2746
Author(s):  
Heng Xin Zhao ◽  
Ming Luo ◽  
Li Xin Mo ◽  
Liang Cheng ◽  
Zheng Ma ◽  
...  

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