Integrated System for High-Throughput Protein Identification Using a Microfabricated Device Coupled to Capillary Electrophoresis/Nanoelectrospray Mass Spectrometry

2001 ◽  
Vol 7 (2) ◽  
pp. 143-155 ◽  
Author(s):  
Jianjun Li ◽  
Tammy-Lynn Tremblay ◽  
Pierre Thibault ◽  
Can Wang ◽  
Said Attiya ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
High Throughput ◽  
Protein Identification ◽  
Integrated System

High Throughput Speciation Analysis of Mercury in Water Environment by Short Column Capillary Electrophoresis On-Line Coupled with Inductively Coupled Plasma Mass Spectrometry

2011 ◽  
Vol 383-390 ◽  
pp. 790-795
Author(s):  
Bao Hui Li ◽  
Bao Juan Tian
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
High Throughput ◽  
Inductively Coupled Plasma ◽  
Speciation Analysis ◽  
Fused Silica ◽  
Short Column ◽  
Inductively Coupled ◽  
Icp Ms ◽  
Plasma Mass Spectrometry

A method for mercury high throughput rapid speciation analysis was built by short column capillary electrophoresis (SC-CE) coupled with inductively coupled plasma mass spectrometry (ICP-MS). A micromist nebulizer was employed to increase the nebulization efficiency and a laboratory-made removable SC-CE-ICP-MS interface on the basis of cross design was applied to alleviate buffer contamination of ICP-MS. In less than 60 s methylmercury (MeHg(I)) and inorganic mercury (Hg(II)) were separated in a 16 × 75 μm i.d. short column fused-silica capillary at 21 kV, while a mixture of 30 mmol/L boric aicd + 5% (v/v) CH3OH (pH=8.60) acted as running electrolyte. The precisions (RSD, n=5) of migration time and peak area for MeHg(I) and Hg(II) were in the range of 1.4-2.6% and 3.3-3.4%, respectively. The limits of detection (3σ) mercury species were 9.7 and 12.0 μg/L, respectively. The recoveries for Hg(II) MeHg(I) were in the range of 96-107% and 99-105%.

scholarly journals Obesity Proteomics: An Update on the Strategies and Tools Employed in the Study of Human Obesity

2018 ◽  
Vol 7 (3) ◽  
pp. 27 ◽  
Author(s):  
Afshan Masood ◽  
Hicham Benabdelkamel ◽  
Assim Alfadda
Keyword(s):  
Mass Spectrometry ◽  
High Throughput ◽  
Large Scale ◽  
Protein Identification ◽  
Biochemical Characterization ◽  
Biological Fluids ◽  
Protein Composition ◽  
Cellular Protein ◽  
Human Obesity ◽  
Two Dimensional Gel Electrophoresis

Proteomics has become one of the most important disciplines for characterizing cellular protein composition, building functional linkages between protein molecules, and providing insight into the mechanisms of biological processes in a high-throughput manner. Mass spectrometry-based proteomic advances have made it possible to study human diseases, including obesity, through the identification and biochemical characterization of alterations in proteins that are associated with it and its comorbidities. A sizeable number of proteomic studies have used the combination of large-scale separation techniques, such as high-resolution two-dimensional gel electrophoresis or liquid chromatography in combination with mass spectrometry, for high-throughput protein identification. These studies have applied proteomics to comprehensive biochemical profiling and comparison studies while using different tissues and biological fluids from patients to demonstrate the physiological or pathological adaptations within their proteomes. Further investigations into these proteome-wide alterations will enable us to not only understand the disease pathophysiology, but also to determine signature proteins that can serve as biomarkers for obesity and related diseases. This review examines the different proteomic techniques used to study human obesity and discusses its successful applications along with its technical limitations.

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